Cellular and molecular outcomes of Pseudomonas putida KT2440 exposure to aluminium
Status Publisher Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články
Grantová podpora
C4000129318 , C4000137308
ESA-BELSPO
CDR J.0071.21
FRFC
Ministère de l'Enseignement Supérieur, de la Recherche Scientifique et des Technologies de l'Information et de la Communication
Ministère de l'Enseignement Supérieur, de la Recherche Scientifique et des Technologies de l'Information et de la Communication
PubMed
41264166
DOI
10.1007/s12223-025-01380-3
PII: 10.1007/s12223-025-01380-3
Knihovny.cz E-zdroje
- Klíčová slova
- Pseudomonas, Aluminium, Bacteria, Biofilm, Metal toxicity, Oxidative stress, Proteomic response,
- Publikační typ
- časopisecké články MeSH
Despite being an abundant metal, nature evolved to exclude aluminium (Al) from living organisms. In addition, the complex chemistry of this element makes it a challenging case for researchers. At physiological pH, Al has strong affinity to oxygen donors and negatively charged molecules such as proteins, nucleotides and cellular components bearing phosphates and carboxylic groups. Because of its widespread industrial use, living organisms are increasingly exposed to soluble forms of this light metal and environmental bacteria are in the front line. In this work, we show the disruptive effect of Al at physiological pH on the cellular morphology of Pseudomonas putida KT2440 and on the integrity of its mature biofilms. Proteomic studies revealed that an exposure to 0.78 mM of the aluminium compound used in this study significantly affected key proteins and enzymes involved in the TCA cycle, the respiratory chain, the maintenance of the cell's membrane and the transmembrane transport systems. The expression levels of major metal-resistance proteins (e.g., P-type ATPases and RND tripartite efflux pumps) was not affected, contrary to those of methyltransferases and systems involved in the metabolism of phosphate that might be involved in the maintenance of low Al concentration in the cytoplasm.
Microbiology Unit Belgian Nuclear Research Centre Nuclear Medical Applications SCK CEN Mol Belgium
National Center for Nuclear Sciences and Technologies Sidi Thabet Tunisia
Proteomics and Microbiology Lab Research Institute for Biosciences Mons University Mons Belgium
Zobrazit více v PubMed
Abdeljelil N, Ben Miloud Yahia N, Landoulsi A, Chatti A, Wattiez R, Gillan D, Van Houdt R (2023) Proteomic and morphological insights into the exposure of Cupriavidus metallidurans CH34 planktonic cells and biofilms to aluminium. J Hazard Mater 465:133403. https://doi.org/10.1016/j.jhazmat.2023.133403 PubMed DOI
Ainsaar K, Mumm K, Ilves H, Hõrak R (2014) The ColRS signal transduction system responds to the excess of external zinc, iron, manganese, and cadmium. BMC Microbiol 14:1–14. https://doi.org/10.1186/1471-2180-14-162 DOI
Alterio, V., Langella, E., De Simone, G., Monti, S.M., 2015. Cadmium-containing carbonic anhydrase CDCA1 in marine diatom Thalassiosira weissflogii. Mar. Drugs 13, 1688–1697. https://doi.org/10.3390/md13041688
Appanna V (1994) Influence of phosphate on aluminum tolerance in Pseudomonas fluorescens. FEMS Microbiol Lett 124:327–332. https://doi.org/10.1016/0378-1097(94)00450-1 DOI
Appanna VD, Hamel R (1996) Aluminum detoxification mechanism in Pseudomonas fluorescens is dependent on iron. FEMS Microbiol Lett 143:223–228. https://doi.org/10.1016/0378-1097(96)00316-3 PubMed DOI
Appanna VD, Kepes M, Rochon P (1994) Aluminum tolerance in Pseudomonas fluorescens ATCC 13525: involvement of a gelatinous lipid-rich residue. FEMS Microbiol Lett 119:295–301. https://doi.org/10.1111/j.1574-6968.1994.tb06904.x DOI
Appanna VD, Pierre MST (1996) Aluminum elicits exocellular phosphatidylethanolamine production in Pseudomonas fluorescens. Appl Environ Microbiol 62(8):2778–2782. https://doi.org/10.1128/aem.62.8.2778-2782.1996 PubMed DOI PMC
Arar M, Bakkour R, Elsner M, Bernstein A (2023) Microbial hydrolysis of atrazine in contaminated groundwater. Chemosphere 322:138226. https://doi.org/10.1016/j.chemosphere.2023.138226 PubMed DOI
Aras A, Rizvanoglu SS, Tanriverdi ES, Karaca B, Eryilmaz M (2023) The effects of antiperspirant aluminum chlorohydrate on the development of antibiotic resistance in Staphylococcus epidermidis. Microorganisms 11:1–13. https://doi.org/10.3390/microorganisms11040948 DOI
Arié JP, Sassoon N, Betton JM (2001) Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol Microbiol 39:199–210. https://doi.org/10.1046/j.1365-2958.2001.02250.x PubMed DOI
Baker TI, Crawford I (1966) Anthranilate synthetase: partial purification and some kinetic studies on the enzyme from Escherichia coli. J Biol Chem 241:5577–5584 PubMed DOI
Bao F, Yan H, Sun H, Yang P, Liu G, Zhou X (2015) Hydrolysis of by-product adenosine diphosphate from 3′-phosphoadenosine-5′-phosphosulfate preparation using nudix hydrolase NudJ. Appl Microbiol Biotechnol 99:10771–10778. https://doi.org/10.1007/s00253-015-6911-8 PubMed DOI
Bennett MS, Guan Z, Laurberg M, Su XD (2001) Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases. Proc Natl Acad Sci U S A 98:13577–13582. https://doi.org/10.1073/pnas.241397198 PubMed DOI PMC
Berg G, Cernava T (2022) The plant microbiota signature of the anthropocene as a challenge for Microbiome research. Microbiome 10:1–12. https://doi.org/10.1186/s40168-021-01224-5 DOI
Berkhout MD, Plugge CM, Belzer C (2022) How microbial glycosyl hydrolase activity in the gut mucosa initiates microbial cross-feeding. Glycobiology 32:182–200. https://doi.org/10.1093/glycob/cwab105 PubMed DOI
Berlemont R, Martiny AC (2015) Genomic potential for polysaccharide deconstruction in bacteria. Appl Environ Microbiol 81:1513–1519. https://doi.org/10.1128/AEM.03718-14 PubMed DOI PMC
Berrisford JM, Baradaran R, Sazanov LA (2016) Structure of bacterial respiratory complex i. Biochimica et Biophysica Acta (BBA) 1857:892–901. https://doi.org/10.1016/j.bbabio.2016.01.012 PubMed DOI
Bjerknes V, Fyllingen I, Holtet L, Teien HC, Rosseland BO, Kroglund F (2003) Aluminium in acidic river water causes mortality of farmed Atlantic salmon (Salmo salar L.) in Norwegian Fjords. Mar Chem 83(3–4):169–174. https://doi.org/10.1016/S0304-4203(03)00110-5 DOI
van Bloois E, Dekker HL, Fröderberg L, Houben ENG, Urbanus ML, de Koster CG, de Gier JW, Luirink J (2008) Detection of cross-links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins. FEBS Lett 582:1419–1424. https://doi.org/10.1016/j.febslet.2008.02.082 PubMed DOI
Boeris PS, Agustín MdelR, Acevedo DF, Lucchesi GI (2016) Biosorption of aluminum through the use of non-viable biomass of Pseudomonas putida. J Biotechnol 236:57–63. https://doi.org/10.1016/j.jbiotec.2016.07.026 PubMed DOI
Boeris PS, Liffourrena AS, Salvano MA, Lucchesi GI (2009) Physiological role of phosphatidylcholine in the Pseudomonas Putida A ATCC 12633 response to tetradecyltrimethylammonium bromide and aluminium. Lett Appl Microbiol 49:491–496. https://doi.org/10.1111/j.1472-765X.2009.02699.x PubMed DOI
Boeris PS, Lucchesi GI (2012) The phosphatidylcholine synthase of Pseudomonas Putida A ATCC 12633 is responsible for the synthesis of phosphatidylcholine, which acts as a temporary reservoir for. Al3+. Microbiology 158:1249–1257. https://doi.org/10.1099/mic.0.054072-0 PubMed DOI
Bonfiglio R, Sisto R, Casciardi S, Palumbo V, Scioli MP, Giacobbi E, Servadei F, Melino G, Mauriello A, Scimeca M (2024) Aluminium bioaccumulation in colon cancer, impinging on epithelial-mesenchymal-transition and cell death. Sci Total Environ 908:168335. https://doi.org/10.1016/j.scitotenv.2023.168335 PubMed DOI
Börner J, Friedrich T, Bartkuhn M, Klug G (2023) Ribonuclease E strongly impacts bacterial adaptation to different growth conditions. RNA Biol 20:120–135. https://doi.org/10.1080/15476286.2023.2195733 PubMed DOI PMC
Bouffartigues E, Gicquel G, Bazire A, Fito-Boncompte L, Taupin L (2011) The major outer membrane protein Oprf is required for rhamnolipid production in Pseudomonas aeruginosa. J Bacteriol Parasitol 02. https://doi.org/10.4172/2155-9597.1000118
Brickman TJ, McIntosh MA (1992) Overexpression and purification of ferric Enterobactin esterase from Escherichia coli: demonstration of enzymatic hydrolysis of Enterobactin and its iron complex. J Biol Chem 267:12350–12355. https://doi.org/10.1016/s0021-9258(19)49846-3 PubMed DOI
Broman E, Sjöstedt J, Pinhassi J, Dopson M (2017) Shifts in coastal sediment oxygenation cause pronounced changes in microbial community composition and associated metabolism. Microbiome 5:96. https://doi.org/10.1186/s40168-017-0311-5 PubMed DOI PMC
Bukhari SI, Aleanizy FS (2020) Association of OprF mutant and disturbance of biofilm and pyocyanin virulence in Pseudomonas aeruginosa. Saudi Pharm J 28:196–200. https://doi.org/10.1016/j.jsps.2019.11.021 PubMed DOI
Burkitt MJ, Wardman P (2001) Cytochrome c is a potent catalyst of dichlorofluorescin oxidation: implications for the role of reactive oxygen species in apoptosis. Biochem Biophys Res Commun 282:329–333. https://doi.org/10.1006/bbrc.2001.4578 PubMed DOI
Butko DA, Wilson EV, Yakovleva EV (2018) The impact of aluminum polynuclear hydroxo complexes on the impurity coagulation in natural water. J Water Chem Technol 40:201–205. https://doi.org/10.3103/s1063455x18040045 DOI
Caillet, S., Millette, M., Dussault, D., Shareck, F., Lacroix, M., 2008. Effect of gamma radiation on heat shock protein expression of four foodborne pathogens. J. Appl. Microbiol. 105, 1384–1391. https://doi.org/10.1111/j.1365-2672.2008.03891.x
Cánovas D, Cases I, De Lorenzo V (2003) Heavy metal tolerance and metal homeostasis in Pseudomonas putida as revealed by complete genome analysis. Environ Microbiol 5:1242–1256. https://doi.org/10.1111/j.1462-2920.2003.00463.x PubMed DOI
Cardiano P, Foti C, Giacobello F, Giuffrè O, Sammartano S (2018) Study of Al3 + interaction with AMP, ADP and ATP in aqueous solution. Biophys Chem 234:42–50. https://doi.org/10.1016/j.bpc.2018.01.003 PubMed DOI
Cardoso, K., Gandra, R.F., Wisniewski, E.S., Osaku, C.A., Kadowaki, M.K., Felipach-Neto, V., Haus, L.F.A.Á., Simão, R.D.C.G., 2010. DnaK and GroEL are induced in response to antibiotic and heat shock in Acinetobacter baumannii. J. Med. Microbiol. 59, 1061–1068. https://doi.org/10.1099/jmm.0.020339-0
Cassin EK, Araujo-Hernandez SA, Baughn DS, Londono MC, Rodriguez DQ, Al-Otaibi NS, Picard A, Bergeron JRC, Tseng BS (2023) OprF impacts Pseudomonas aeruginosa biofilm matrix eDNA levels in a nutrient-dependent manner. J Bacteriol. https://doi.org/10.1128/jb.00080-23 PubMed DOI PMC
Chandra J, Parkhey S, Varghese D, Sershen, Varghese B, Keshavkant S (2020) Aluminium rhizotoxicity in Cicer arietinum. Russ J Plant Physiol 67:945–952. https://doi.org/10.1134/S1021443720050027 DOI
Chaudhuri G, Venu-Babu P, Dalal D, Thilagaraj WR (2015) Application of alkaline phosphatase for heavy metals precipitation using ascorbic acid 2-phosphate as an effective natural substrate. Int J Environ Sci Technol 12:3877–3886. https://doi.org/10.1007/s13762-014-0749-y DOI
Chen S, Bleam WF, Hickey WJ (2010) Molecular analysis of two bacterioferritin genes, Bfra and bfrβ, in the model rhizobacterium Pseudomonas Putida KT2440. Appl Environ Microbiol 76:5335–5343. https://doi.org/10.1128/AEM.00215-10 PubMed DOI PMC
Cheng VWT, Ma E, Zhao Z, Rothery RA, Weiner JH (2006) The iron-sulfur clusters in Escherichia coli succinate dehydrogenase direct electron flow. J Biol Chem 281:27662–27668. https://doi.org/10.1074/jbc.M604900200 PubMed DOI
Chenier D, Beriault R, Mailloux R, Baquie M, Abramia G, Lemire J, Appanna V (2008) Involvement of fumarase C and NADH oxidase in metabolic adaptation of Pseudomonas fluorescens cells evoked by aluminum and gallium toxicity. Appl Environ Microbiol 74:3977–3984. https://doi.org/10.1128/AEM.02702-07 PubMed DOI PMC
Chevalier S, Bouffartigues E, Bodilis J, Maillot O, Lesouhaitier O, Feuilloley MGJ, Orange N, Dufour A, Cornelis P (2017) Structure, function and regulation of Pseudomonas aeruginosa porins. FEMS Microbiol Rev 41:698–722. https://doi.org/10.1093/femsre/fux020 PubMed DOI
Chiba S, Ito K, Akiyama Y (2006) The Escherichia coli plasma membrane contains two PHB (prohibitin homology) domain protein complexes of opposite orientations. Mol Microbiol 60:448–457. https://doi.org/10.1111/j.1365-2958.2006.05104.x PubMed DOI
Chong YH, Suh YH (1995) Aggregation of amyloid precursor proteins by aluminum in vitro. Brain Res 670:137–141. https://doi.org/10.1016/0006-8993(94)01304-Z PubMed DOI
Chuang SE, Blattner FR (1993) Characterization of twenty-six new heat shock genes of Escherichia coli. J Bacteriol 175:5242–5252. https://doi.org/10.1128/jb.175.16.5242-5252.1993 PubMed DOI PMC
Costa-Gutierrez SB, Raimondo EE, Vincent PA, de Cristóbal RE (2023) Importance of biofilm formation for promoting plant growth under salt stress in Pseudomonas putida KT2440. J Basic Microbiol 63:1219–1232. https://doi.org/10.1002/jobm.202300215 PubMed DOI
Coudray N, Isom GL, Macrae MR, Saiduddin MN, Bhabha G, Ekiert DC (2020) Structure of bacterial phospholipid transporter MlaFEDB with substrate bound. Elife 9:1–73. https://doi.org/10.7554/eLife.62518 DOI
Crabbé A, Leroy B, Wattiez R, Aertsen A, Leys N, Cornelis P, Van Houdt R (2012) Differential proteomics and physiology of Pseudomonasputida KT2440 under filament-inducing conditions. BMC Microbiol. https://doi.org/10.1186/1471-2180-12-282 PubMed DOI PMC
Cui X, Huo M, Chen C, Yu Z, Zhou C, Li A, Qiao B, Zhou D, Crittenden JC (2018) Low concentrations of Al(III) accelerate the formation of biofilm: multiple effects of hormesis and flocculation. Sci Total Environ 634:516–524. https://doi.org/10.1016/j.scitotenv.2018.03.376 PubMed DOI
Dartigalongue C, Raina S (1998) A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J 17:3968–3980. https://doi.org/10.1093/emboj/17.14.3968 PubMed DOI PMC
Dewachter L, Verstraeten N, Monteyne D, Kint CI, Versées W, Pérez-Morga D, Michiels J, Fauvart M (2015) A single-amino-acid substitution in Obg activates a new programmed cell death pathway in Escherichia coli. MBio 6:6–11. https://doi.org/10.1128/mBio.01935-15 DOI
Donlan RM (2000) Role of biofilms in antimicrobial resistance: ASAIO journal. ASAIO J 46:S47-52 PubMed DOI
Dosunmu E, Chaudhari AA, Singh SR, Dennis VA, Pillai SR (2015) Silver-coated carbon nanotubes downregulate the expression of Pseudomonas aeruginosa virulence genes: A potential mechanism for their antimicrobial effect. Int J Nanomed 10:5025–5034. https://doi.org/10.2147/IJN.S85219 DOI
Dougan DA (2013) Regulated proteolysis in microorganisms, Subcellular Biochemistry
Duan K, Lafontaine ER, Majumdar S, Sokol PA (2000) RegA, iron, and growth phase regulate expression of the Pseudomonas aeruginosa tol-oprL gene cluster. J Bacteriol 182:2077–2087. https://doi.org/10.1128/JB.182.8.2077-2087.2000 PubMed DOI PMC
Erhardt H, Steimle S, Muders V, Pohl T, Walter J, Friedrich T (2012) Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli. Biochimica et Biophysica Acta (BBA) 1817:863–871. https://doi.org/10.1016/j.bbabio.2011.10.008 PubMed DOI
Esser L, Zhou F, Yu CA, Xia D (2019) Crystal structure of bacterial cytochrome bc1 in complex with azoxystrobin reveals a conformational switch of the Rieske iron–sulfur protein subunit. J Biol Chem 294:12007–12019. https://doi.org/10.1074/jbc.RA119.008381 PubMed DOI PMC
Figaj D, Ambroziak P, Przepiora T, Skorko-Glonek J (2019) The role of proteases in the virulence of plant pathogenic bacteria. Int J Mol Sci. https://doi.org/10.3390/ijms20030672 PubMed DOI PMC
Flemming HC, Wingender J (2010) The biofilm matrix. Nat Rev Microbiol 8:623–633. https://doi.org/10.1038/nrmicro2415 PubMed DOI
Frenk S, Ben-Moshe T, Dror I, Berkowitz B, Minz D (2013) Effect of metal oxide nanoparticles on microbial community structure and function in two different soil types. PLoS ONE 8:1–12. https://doi.org/10.1371/journal.pone.0084441 DOI
Furrer G, Trusch B, Müller C (1992) The formation of polynuclear Al13 under simulated natural conditions. Geochim Cosmochim Acta 56:3831–3838. https://doi.org/10.1016/0016-7037(92)90174-H DOI
Gage M, Vinithakumari AA, Mooyottu S, Thippeswamy T (2022) Gut dysbiosis following organophosphate, diisopropylfluorophosphate (DFP), intoxication and Saracatinib oral administration. Front Microbiolomes 1:1–15. https://doi.org/10.3389/frmbi.2022.1006078 DOI
Ge F, Sun J, Ren Y, He B, Li J, Yang S, Li W (2022) Transcriptomic and enzymatic analysis reveals the roles of glutamate dehydrogenase in Corynebacterium glutamicum. AMB Express. https://doi.org/10.1186/s13568-022-01506-7 PubMed DOI PMC
González-López MA, Velázquez-Guadarrama N, Romero-Espejel ME, Olivares-Trejo JDJ (2013) Helicobacter pylori secretes the chaperonin GroEL (HSP60), which binds iron. FEBS Lett 587:1823–1828. https://doi.org/10.1016/j.febslet.2013.04.048 PubMed DOI
Green VS, Stott DE, Diack M (2006) Assay for fluorescein diacetate hydrolytic activity: optimization for soil samples. Soil Biol Biochem 38:693–701. https://doi.org/10.1016/j.soilbio.2005.06.020 DOI
Guida L, Saidi Z, Hughes MN, Poole RK (1991) Aluminium toxicity and binding to 507–512
Hamel R, Appanna VD (2003) Aluminum detoxification in Pseudomonas fluorescens is mediated by oxalate and phosphatidylethanolamine. Biochimica et Biophysica Acta (BBA) 1619:70–76. https://doi.org/10.1016/S0304-4165(02)00444-0 PubMed DOI
Han G, Mannaa M, Jeon H, Jung H, Kim JC, Park AR, Seo YS (2022) Dysbiosis in the rhizosphere microbiome of standing dead Korean fir (Abies koreana). Plants. https://doi.org/10.3390/plants11070990 PubMed DOI PMC
Haritha A, Sagar KP, Tiwari A, Kiranmayi P, Rodrigue A, Mohan PM, Singh SS (2009) MrdH, a novel metal resistance determinant of Pseudomonas putida KT2440, is flanked by metal-inducible mobile genetic elements. J Bacteriol 191:5976–5987. https://doi.org/10.1128/JB.00465-09 PubMed DOI PMC
Halsted MC, Bible AN, Morrell-Falvey JL, Retterer ST (2020) Quantifying biofilm propagation on chemically modified surfaces. bioRxiv
Hempel SL, Buettner GR, O’Malley YQ, Wessels DA, Flaherty DM (1999) Dihydrofluorescein diacetate is superior for detecting intracellular oxidants: comparison with 2’,7’-dichlorodihydrofluorescein diacetate, 5(and 6)-carboxy-2’,7’-dichlorodihydrofluorescein diacetate, and dihydrorhodamine 123. Free Radic Biol Med 27:146–159. https://doi.org/10.1016/S0891-5849(99)00061-1 PubMed DOI
Hennequin, C., Collignon, A., Karjalainen, T., 2001. Analysis of expression of GroEL (Hsp60) of Clostridium difficile in response to stress. Microb. Pathog. 31, 255–260. https://doi.org/10.1006/mpat.2001.0468
Henríquez T, Hsu J-S, Hernandez JS, Kuppermann S, Eder M, Jung H (2023) Contribution of uncharacterized target genes of MxtR/ErdR to carbon source utilization by Pseudomonas Putida KT2440. Microbiol Spectr. https://doi.org/10.1128/spectrum.02923-22 PubMed DOI
Hollmann A, Martinez M, Maturana P, Semorile LC, Maffia PC (2018) Antimicrobial peptides: interaction with model and biological membranes and synergism with chemical antibiotics. Front Chem 6:1–13. https://doi.org/10.3389/fchem.2018.00204 DOI
Huang G, Hou Q, Han D, Liu R, Song J (2023) Large scale occurrence of aluminium-rich shallow groundwater in the Pearl River Delta after the rapid urbanization: co-effects of anthropogenic and geogenic factors. J Contam Hydrol 254:104130. https://doi.org/10.1016/j.jconhyd.2022.104130 PubMed DOI
Illmer P, Buttinger R (2006) Interactions between iron availability, aluminium toxicity and fungal siderophores. Biometals 19:367–377. https://doi.org/10.1007/s10534-005-3496-1 PubMed DOI
Jigyasu DK, Kuvar R (2015) High mobility of aluminium in gomati river basin: implications to human health. Curr Sci Association Stable 108:434–438
Kadam MS, Burra VLSP (2023) S-adenosyl-l-methionine interaction signatures in methyltransferases. J Biomol Struct Dyn 0:1. https://doi.org/10.1080/07391102.2023.2217679 DOI
Karlik SJ, Eichhorn GL (1989) Polynucleotide cross-linking by aluminum. J Inorg Biochem 37:259–269. https://doi.org/10.1016/0162-0134(89)85001-9 PubMed DOI
Kawahara M, Kato M, Kuroda Y (2001) Effects of aluminum on the neurotoxicity of primary cultured neurons and on the aggregation of β-amyloid protein. Brain Res Bull 55:211–217. https://doi.org/10.1016/S0361-9230(01)00475-0 PubMed DOI
Kawahara M, Kato-Negishi M (2011) Link between aluminum and the pathogenesis of Alzheimer’s disease: the integration of the aluminum and amyloid cascade hypotheses. Int J Alzheimers Dis. https://doi.org/10.4061/2011/276393 PubMed DOI PMC
Keohane CE, Steele AD, Fetzer C, Khowsathit J, Tyne V, Gilmore MS, Karanicolas J, Stephan A, Wuest WM, States U, Program T, Chase F, States U, Eye M, Infirmary E, States U, States U, Oxford H, Scotland F, Kingdom U (2019) Promysalin elicits species-selective Inhibition of Pseudomonas aeruginosa by targeting succinate dehydrogenase. J Am Chem Soc 140:1774–1782. https://doi.org/10.1021/jacs.7b11212.Promysalin DOI
Kim J, Hong H, Heo A, Park W (2013) Indole toxicity involves the inhibition of adenosine triphosphate production and protein folding in Pseudomonas Putida. FEMS Microbiol Lett 343:89–99. https://doi.org/10.1111/1574-6968.12135 PubMed DOI
Kiss T, Zatta P, Corain B (1996) Interaction of aluminium(III) with phosphate-binding sites: biological aspects and implications. Coord Chem Rev 149:329–346. https://doi.org/10.1016/s0010-8545(96)90036-3 DOI
Kitagawa M, Miyakawa M, Matsumura Y, Tsuchido T (2002) Escherichia coli small heat shock proteins, IbpA and IbpB, protect enzymes from inactivation by heat and oxidants. Eur J Biochem 269:2907–2917. https://doi.org/10.1046/j.1432-1033.2002.02958.x PubMed DOI
Kivistik PA, Putrinš M, Püvi K, Ilves H, Kivisaar M, Hõrak R (2006) The ColRS two-component system regulates membrane functions and protects Pseudomonas putida against phenol. J Bacteriol 188:8109–8117. https://doi.org/10.1128/JB.01262-06 PubMed DOI PMC
Kobayashi G, Moriya S, Wada C (2001) Deficiency of essential GTP-binding protein obge in Escherichia coli inhibits chromosome partition. Mol Microbiol 41:1037–1051. https://doi.org/10.1046/j.1365-2958.2001.02574.x PubMed DOI
Kolata P, Efremov RG (2021) Structure of Escherichia coli respiratory complex i reconstituted into lipid nanodiscs reveals an uncoupled conformation. Elife 10:1–32. https://doi.org/10.7554/eLife.68710 DOI
Kong Y, Ma Y, Ding L, Ma J, Zhang H, Chen Z, Shen J (2021) Coagulation behaviors of aluminum salts towards humic acid: detailed analysis of aluminum speciation and transformation. Sep Purif Technol 259:118137. https://doi.org/10.1016/j.seppur.2020.118137 DOI
Krajewski SS, Joswig M, Nagel M, Narberhaus F (2014) A tricistronic heat shock operon is important for stress tolerance of Pseudomonas putida and conserved in many environmental bacteria. Environ Microbiol 16:1835–1853. https://doi.org/10.1111/1462-2920.12432 PubMed DOI
Lane, T.W., Morel, F.M.M., 2000. A biological function for cadmium in marine diatoms. Proc. Natl. Acad. Sci. U. S. A. 97, 4627–4631. https://doi.org/10.1073/pnas.090091397
Larson SL, Ballard JH, Runge KA, Zhang H, Breland BR, Nick ZH, Vroman ET, Weiss CA, Han FX (2023) Effects of aluminum ion on particle sizes and surface charges of exopolysaccharides from Rhizobium tropici and pH effects. Rhizosphere 26:100713. https://doi.org/10.1016/j.rhisph.2023.100713 DOI
Leedjärv A, Ivask A, Virta M (2008) Interplay of different transporters in the mediation of divalent heavy metal resistance in Pseudomonas Putida KT2440. J Bacteriol 190:2680–2689. https://doi.org/10.1128/JB.01494-07 PubMed DOI
Lin J, Cheng J, Wang Y, Shen X (2018) The Pseudomonas quinolone signal (PQS): not just for quorum sensing anymore. Front Cell Infect Microbiol 8:1–9. https://doi.org/10.3389/fcimb.2018.00230 DOI
Lin YM, Wu SJ, Chang TW, Wang CF, Suen CS, Hwang MJ, Chang MDT, Chen YT, Liao Y, Di (2010) Outer membrane protein I of Pseudomonas aeruginosa is a target of cationic antimicrobial peptide/protein. J Biol Chem 285:8985–8994. https://doi.org/10.1074/jbc.M109.078725 PubMed DOI PMC
Linton KJ, Higgins CF (1998) The Escherichia coli ATP-binding cassette (ABC) proteins. Mol Microbiol 28:5–13 PubMed DOI
Liu H, Li S, Xie X, Shi Q (2021) Pseudomonas putida actively forms biofilms to protect the population under antibiotic stress. Environ Pollut 270:116261. https://doi.org/10.1016/j.envpol.2020.116261 PubMed DOI
Liu H, Zhu R, Shu K, Lv W, Wang S, Wang C (2022) Aluminum stress signaling, response, and adaptive mechanisms in plants. Plant Signal Behav. https://doi.org/10.1080/15592324.2022.2057060 PubMed DOI PMC
Llamas MA, Rodríguez-Herva JJ, Hancock REW, Bitter W, Tommassen J, Ramos JL (2003) Role of Pseudomonas putida tol-oprL gene products in uptake of solutes through the cytoplasmic membrane. J Bacteriol 185:4707–4716. https://doi.org/10.1128/JB.185.16.4707-4716.2003 PubMed DOI PMC
Lu CD, Abdelal AT (2001) The GdhB gene of Pseudomonas aeruginosa encodes an arginine-inducible NAD+-dependent glutamate dehydrogenase which is subject to allosteric regulation. J Bacteriol 183:490–499. https://doi.org/10.1128/JB.183.2.490-499.2001 PubMed DOI PMC
Macaskie LE, Bonthrone KM, Rouch DA (1994) Phosphatase-mediated heavy metal accumulation by a Citrobacter sp. and related Enterobacteria. FEMS Microbiol Lett 121:141–146. https://doi.org/10.1111/j.1574-6968.1994.tb07090.x PubMed DOI
Mahmoud SA, Chien P (2018) Regulated proteolysis in bacteria. Annu Rev Biochem 87:677–696. https://doi.org/10.1146/annurev-biochem-062917-012848 PubMed DOI PMC
Malinverni JC, Silhavy TJ (2009) An ABC transport system that maintains lipid asymmetry in the Gram-negative outer membrane. Proc Natl Acad Sci USA 106:8009–8014. https://doi.org/10.1073/pnas.0903229106 PubMed DOI PMC
Manara A, Dalcorso G, Baliardini C, Farinati S, Cecconi D, Furini A (2012) Pseudomonas putida response to cadmium: changes in membrane and cytosolic proteomes. J Proteome Res 11:4169–4179. https://doi.org/10.1021/pr300281f PubMed DOI
Manasherob R, Miller C, Kim K, sun, Cohen SN (2012) Ribonuclease E modulation of the bacterial SOS response. PLoS One 7. https://doi.org/10.1371/journal.pone.0038426
Mandriota SJ, Tenan M, Ferrari P, Sappino AP (2016) Aluminium chloride promotes tumorigenesis and metastasis in normal murine mammary gland epithelial cells. Int J Cancer 139:2781–2790. https://doi.org/10.1002/ijc.30393 PubMed DOI PMC
Martins M, Taborda R, Silva G, Assunção A, Matos AP, Costa MC (2012) Aluminum and sulphate removal by a highly Al-resistant dissimilatory sulphate-reducing bacteria community. Biodegradation 23:693–703. https://doi.org/10.1007/s10532-012-9545-x PubMed DOI
Matuszewska E, Kwiatkowska J, Kuczyńska-Wiśnik D, Laskowska E (2008) Escherichia coli heat-shock proteins IbpA/B are involved in resistance to oxidative stress induced by copper. Microbiology 154:1739–1747. https://doi.org/10.1099/mic.0.2007/014696-0 PubMed DOI
Mergeay, M., Nies, D., Schlegel, H.G., Gerits, J., Charles, P., Van Gijsegem, F., 1985. Alcaligenes eutrophus CH34 is a facultative chemolithotroph with plasmid-bound resistance to heavy metals. J. Bacteriol. 162, 328–334
Meyer JM (1992) Exogenous siderophore-mediated iron uptake in Pseudomonas aeruginosa: possible involvement of porin OprF in iron translocation. J Gen Microbiol 138:951–958. https://doi.org/10.1099/00221287-138-5-951 PubMed DOI
Michta, E., Ding, W., Zhu, S., Blin, K., Ruan, H., Wang, R., Wohlleben, W., Mast, Y., 2014. Proteomic approach to reveal the regulatory function of aconitase AcnA in oxidative stress response in the antibiotic producer Streptomyces viridochromogenes Tü494. PLoS One 9. https://doi.org/10.1371/journal.pone.0087905
Middaugh J, Hamel R, Jean-Baptiste G, Beriault R, Chenier D, Appanna VD (2005) Aluminum triggers decreased aconitase activity via Fe-S cluster disruption and the overexpression of isocitrate dehydrogenase and isocitrate lyase: A metabolic network mediating cellular survival. J Biol Chem 280:3159–3165. https://doi.org/10.1074/jbc.M411979200 PubMed DOI
Missiakas D, Schwager F, Betton JM, Georgopoulos C, Raina S (1996) Identification and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J 15:6899–6909. https://doi.org/10.1002/j.1460-2075.1996.tb01082.x PubMed DOI PMC
Molina LÁ, Ramos C, Duque E, Ronchel MC, García JM, Wyke L, Ramos JL (2000) Survival of Pseudomonas Putida KT2440 in soil and in the rhizosphere of plants under greenhouse and environmental conditions. Soil Biol Biochem 32:315–321. https://doi.org/10.1016/S0038-0717(99)00156-X DOI
Monds RD, Newell PD, Schwartzman JA, O’Toole GA (2006) Conservation of the Pho Regulon in Pseudomonas fluorescens Pf0-1. Appl Environ Microbiol 72:1910–1924. https://doi.org/10.1128/AEM.72.3.1910-1924.2006 PubMed DOI PMC
Mousavi SE, Delgado-Saborit JM, Adivi A, Pauwels S, Godderis L (2022) Air pollution and endocrine disruptors induce human microbiome imbalances: a systematic review of recent evidence and possible biological mechanisms. Sci Total Environ 816:151654. https://doi.org/10.1016/j.scitotenv.2021.151654 PubMed DOI
Mozumder AB, Chanda K, Chorei R, Prasad HK (2022) An evaluation of aluminum tolerant Pseudomonas aeruginosa A7 for in vivo suppression of fusarium wilt of Chickpea caused by Fusarium oxysporum f. sp. ciceris and growth promotion of Chickpea. Microorganisms. https://doi.org/10.3390/microorganisms10030568 PubMed DOI PMC
Mraheil MA, Billion A, Mohamed W, Rawool D, Hain T, Chakraborty T (2011) Adaptation of Listeria monocytogenes to oxidative and nitrosative stress in IFN-γ-activated macrophages. Int J Med Microbiol 301:547–555. https://doi.org/10.1016/j.ijmm.2011.05.001 PubMed DOI
Navare AT, Chavez JD, Zheng C, Weisbrod CR, Eng JK, Siehnel R, Singh PK, Manoil C, Bruce JE (2015) Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry. Structure 23:762–773. https://doi.org/10.1016/j.str.2015.01.022 PubMed DOI PMC
Nelson KE, Weinel C, Paulsen IT, Dodson RJ, Hilbert H, Santos VAPM, Fouts DE, Gill SR, Pop M, Holmes M, Brinkac L, Beanan M, Deboy RT, Daugherty S, Kolonay J, Madupu R, Nelson W, White O, Peterson J, Khouri H, Hance I, Lee PC, Holtzapple E, Scanlan D, Tran K, Moazzez A, Utterback T, Rizzo M, Lee K, Kosack D, Moestl D, Wedler H, Lauber J, Stjepandic D, Hoheisel J, Straetz M, Heim S, Kiewitz C, Eisen J, Timmis KN, Düsterhöft A, Tümmler B, Fraser CM (2002) Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas Putida KT 2440(4):799–808. https://doi.org/10.1046/j.1462-2920.2002.00366.x
Nikel PI, Kim J, de Lorenzo V (2014) Metabolic and regulatory rearrangements underlying glycerol metabolism in Pseudomonas putida KT2440. Environ Microbiol 16:239–254. https://doi.org/10.1111/1462-2920.12224 PubMed DOI
Nurzhan A, Tian H, Nuralykyzy B, He W (2022) Soil enzyme activities and enzyme activity indices in long-term arsenic-contaminated soils. Eurasian Soil Sci 55:1425–1435. https://doi.org/10.1134/S106422932210012X DOI
Obruca S, Sedlacek P, Koller M, Kucera D, Pernicova I (2018) Involvement of polyhydroxyalkanoates in stress resistance of microbial cells: biotechnological consequences and applications. Biotechnol Adv 36:856–870. https://doi.org/10.1016/j.biotechadv.2017.12.006 PubMed DOI
Pabst MJ, Kuhn JC, Somerville RL (1973) Feedback regulation in the anthranilate aggregate from wild type and mutant strains of Escherichia coli. J Biol Chem 248:901–914. https://doi.org/10.1016/s0021-9258(19)44352-4 PubMed DOI
Paerl HW, Dyble J, Moisander PH, Noble RT, Piehler MF, Pinckney JL, Steppe TF, Twomey L, Valdes LM (2003) Microbial indicators of aquatic ecosystem change: current applications to eutrophication studies. FEMS Microbiol Ecol 46:233–246. https://doi.org/10.1016/S0168-6496(03)00200-9 PubMed DOI
Pakrashi S, Dalai S, Trivedi TCP, Myneni S, Raichur R, Chandrasekaran AM, Mukherjee N, A (2013) Cytotoxicity of aluminium oxide nanoparticles towards fresh water algal isolate at low exposure concentrations. Aquat Toxicol 132–133. https://doi.org/10.1016/j.aquatox.2013.01.018
Panmanee W, Gomez F, Witte D, Pancholi V, Britigan BE, Hassett DJ (2008) The peptidoglycan-associated lipoprotein OprL helps protect a Pseudomonas aeruginosa mutant devoid of the transactivator OxyR from hydrogen peroxide-mediated killing during planktonic and biofilm culture. J Bacteriol 190:3658–3669. https://doi.org/10.1128/JB.00022-08 PubMed DOI PMC
Park SJ, Chao G, Gunsalus RP (1997) Aerobic regulation of the SucABCD genes of Escherichia coli, which encode α-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream SdhCDAB promoter. J Bacteriol 179:4138–4142. https://doi.org/10.1128/jb.179.13.4138-4142.1997 PubMed DOI PMC
Pérez G, Garbossa G, Di Risio C, Vittori D, Nesse A (2001) Disturbance of cellular iron uptake and utilisation by aluminium. J Inorg Biochem 87(1–2):21–27. https://doi.org/10.1016/S0162-0134(01)00310-5 PubMed DOI
Pérez G, Pregi N, Vittori D, Di Risio C, Garbossa G, Nesse A (2005) Aluminum exposure affects transferrin-dependent and -independent iron uptake by K562 cells. Biochimica et Biophysica Acta (BBA) 1745:124–130. https://doi.org/10.1016/j.bbamcr.2004.12.002 PubMed DOI
Persky NS, Ferullo DJ, Cooper DL, Moore HR, Lovett ST (2009) The ObgE/CgtA GTPase influences the stringent response to amino acid starvation in Escherichia coli. Mol Microbiol 73:253–266. https://doi.org/10.1111/j.1365-2958.2009.06767.x PubMed DOI PMC
Poblete-Castro I, Aravena-Carrasco C, Orellana-Saez M, Pacheco N, Cabrera A, Borrero-de Acuña JM (2020) Engineering the osmotic state of Pseudomonas Putida KT2440 for efficient cell disruption and downstream processing of poly(3-hydroxyalkanoates). Front Bioeng Biotechnol 8. https://doi.org/10.3389/fbioe.2020.00161
Poléo ABS (1995) Aluminium polymerization - a mechanism of acute toxicity of aqueous aluminium to fish. Aquat Toxicol 31:347–356. https://doi.org/10.1016/0166-445X(94)00083-3 DOI
Purwanti IF, Kurniawan SB, Imron MF (2019) Potential of Pseudomonas aeruginosa isolated from aluminium-contaminated site in aluminium removal and recovery from wastewater. Environ Technol Innov 15:100422. https://doi.org/10.1016/j.eti.2019.100422 DOI
Qi Q, Rehm BHA, Steinbüchel A (1997) Synthesis of poly(3-hydroxyalkanoates) in Escherichia coli expressing the PHA synthase gene phaC2 from Pseudomonas aeruginosa: comparison of PhaC1 and PhaC2. FEMS Microbiol Lett 157:155–162. https://doi.org/10.1016/S0378-1097(97)00469-2 PubMed DOI
Queener SW, Queener SF, Meeks JR, Gunsalus IC (1973) Anthranilate synthase from Pseudomonas putida. J Biol Chem 248:151–161. https://doi.org/10.1016/s0021-9258(19)44457-8 PubMed DOI
Rasamiravaka T, Ngezahayo J, Pottier L, Ribeiro SO, Souard F, Hari L, Stévigny C, El Jaziri M, Duez P (2017) Terpenoids from Platostoma rotundifolium (Briq.) A. J. paton alter the expression of quorum sensing-related virulence factors and the formation of biofilm in Pseudomonas aeruginosa PAO1. Int J Mol Sci 18. https://doi.org/10.3390/ijms18061270
Rodríguez-Herva JJ, Ramos JL (1996) Characterization of an OprL null mutant of Pseudomonas putida. J Bacteriol 178:5836–5840. https://doi.org/10.1128/jb.178.19.5836-5840.1996 PubMed DOI PMC
Roosa S, Wauven C, Vander, Billon G, Matthijs S, Wattiez R, Gillan DC (2014) The Pseudomonas community in metal-contaminated sediments as revealed by quantitative PCR: A link with metal bioavailability. Res Microbiol 165:647–656. https://doi.org/10.1016/j.resmic.2014.07.011 PubMed DOI
Sarkar B, Saha I, De AK, Ghosh A, Adak MK (2020) Aluminium accumulation in excess and related anti-oxidation responses in C4 weed (Amaranthus viridis L.). Physiol Mol Biol Plants 26:1583–1598. https://doi.org/10.1007/s12298-020-00840-z PubMed DOI PMC
Saul FA, Arié JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA (2004) Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J Mol Biol 335:595–608. https://doi.org/10.1016/j.jmb.2003.10.056 PubMed DOI
Ščančar J, Milačič R (2006) Aluminium speciation in environmental samples: a review. Anal Bioanal Chem 386:999–1012. https://doi.org/10.1007/s00216-006-0422-5 PubMed DOI
Scott JM, Haldenwang WG (1999) Obg, an essential GTP binding protein of Bacillus subtilis, is necessary for stress activation of transcription factor σ(B). J Bacteriol 181:4653–4660. https://doi.org/10.1128/jb.181.15.4653-4660.1999 PubMed DOI PMC
Slyemi D, Bonnefoy V (2012) How prokaryotes deal with arsenic. Environ Microbiol Rep 4:571–586. https://doi.org/10.1111/j.1758-2229.2011.00300.x PubMed DOI
Sterling SM, MacLeod S, Rotteveel L, Hart K, Clair TA, Halfyard EA, O’Brien NL (2020) Ionic aluminium concentrations exceed thresholds for aquatic health in Nova Scotian rivers, even during conditions of high dissolved organic carbon and low flow. Hydrol Earth Syst Sci 24:4763–4775. https://doi.org/10.5194/hess-24-4763-2020 DOI
Swanson, M.A., Usselman, R.J., Frerman, F.E., Eaton, G.R., Eaton, S.S., 2008. The Iron-Sulfur Cluster of Electron Transfer Flavoproteinubiquinone Oxidoreductase (ETF-QO) is the Electron Acceptor for Electron Transfer Flavoprotein. Biochemistry 47, 8894–8901. https://doi.org/10.1021/bi800507p
Szabó P, Jordan G, Kocsis T, Posta K, Kardos L, Šajn R, Alijagić J (2022) Biomonitoring and assessment of toxic element contamination in floodplain sediments and soils using fluorescein diacetate (FDA) enzymatic activity measurements: evaluation of possibilities and limitations through the case study of the Drava river floodpla. Environ Monit Assess. https://doi.org/10.1007/s10661-022-10301-7 PubMed DOI PMC
Szczepaniak J, Press C, Kleanthous C (2020) The multifarious roles of Tol-Pal in Gram-negative bacteria. FEMS Microbiol Rev 44:490–506. https://doi.org/10.1093/femsre/fuaa018 PubMed DOI PMC
Tamás L, Huttová J, Mistrík I, Šimonovičová M, Široká B (2005) Aluminium induced esterase activity and isozyme pattern in barley root tip. Plant Soil Environ 51:220–225. https://doi.org/10.17221/3577-pse DOI
Tamber S, Ochs MM, Hancock REW (2006) Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa. J Bacteriol 188:45–54. https://doi.org/10.1128/JB.188.1.45-54.2006 PubMed DOI PMC
Teitzel GM, Geddie A, De Long SK, Kirisits MJ, Whiteley M, Parsek MR (2006) Survival and growth in the presence of elevated copper: transcriptional profiling of copper-stressed Pseudomonas aeruginosa. J Bacteriol 188:7242–7256. https://doi.org/10.1128/JB.00837-06 PubMed DOI PMC
Teitzel GM, Parsek MR (2003) Heavy metal resistance of biofilm and planktonic Pseudomonas aeruginosa. Appl Environ Microbiol 69:2313–2320. https://doi.org/10.1128/AEM.69.4.2313-2320.2003 PubMed DOI PMC
Theriot CM, Grunden AM (2011) Hydrolysis of organophosphorus compounds by microbial enzymes. Appl Microbiol Biotechnol 89:35–43. https://doi.org/10.1007/s00253-010-2807-9 PubMed DOI
Thong S, Ercan B, Torta F, Fong ZY, Alvina Wong HY, Wenk MR, Chng SS (2016) Defining key roles for auxiliary proteins in an ABC transporter that maintains bacterial outer membrane lipid asymmetry. Elife 5:1–19. https://doi.org/10.7554/eLife.19042 DOI
Tumlirsch T, Jendrossek D (2017) Proteins with CHADs (Conserved histidine -helical domains) are attached to polyphosphate granules in vivo and constitute a novel family of polyphosphate-associated proteins (phosins). Appl Environ Microbiol 83:1–14 DOI
Ünal CM, Steinert M (2014) Microbial peptidyl-prolyl cis / trans isomerases (PPIases): virulence factors and potential alternative drug targets. Microbiol Mol Biol Rev 78:544–571. https://doi.org/10.1128/mmbr.00015-14 PubMed DOI PMC
Uthus, E.O., 1992. Evidence for arsenic essentiality. Environ. Geochem. Health 14, 55–58. https://doi.org/10.1007/BF01783629
Vermassen A, Leroy S, Talon R, Provot C, Popowska M, Desvaux M (2019) Cell wall hydrolases in bacteria: insight on the diversity of cell wall amidases, glycosidases and peptidases toward peptidoglycan. Front Microbiol. https://doi.org/10.3389/fmicb.2019.00331 PubMed DOI PMC
Vílchez S, Manzanera M, Ramos JL (2000) Control of expression of divergent Pseudomonas Putida put promoters for proline catabolism. Appl Environ Microbiol 66:5221–5225. https://doi.org/10.1128/AEM.66.12.5221-5225.2000 PubMed DOI PMC
Waite CC, da Silva C, Bitencourt GOA, Sabadini-Santos JAP, Crapez E, M.A.C (2016) Copper and lead removal from aqueous solutions by bacterial consortia acting as biosorbents. Mar Pollut Bull 109:386–392. https://doi.org/10.1016/j.marpolbul.2016.05.044 PubMed DOI
Wang B, Wu C, Cui L, Wang H, Liu Y, Cui W (2022) Dietary aluminium intake disrupts the overall structure of gut microbiota in Wistar rats. Food Sci Nutr 10:3574–3584. https://doi.org/10.1002/fsn3.2955 PubMed DOI PMC
Wang H, Joseph JA (1999) Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader. Free Radic Biol Med 27:612–616 PubMed DOI
Wang S, Liu X, Liu H, Zhang L, Guo Y, Yu S, Daniel J, Biology MI (2015) The exopolysaccharide Psl–eDNA interaction enables the formation of a biofilm skeleton in. Pseudomonas Aeruginosa Shiwei 7:330–340. https://doi.org/10.1111/1758-2229.12252.The DOI
Wang W, Yang H, Wang X, Jiang J, Zhu W (2010) Effects of fulvic acid and humic acid on aluminum speciation in drinking water. J Environ Sci (China) 22:211–217. https://doi.org/10.1016/S1001-0742(09)60095-4 PubMed DOI
Watanabe S, Stazic D, Georg J, Ohtake S, Sakamaki Y, Numakura M, Asayama M, Chibazakura T, Wilde A, Steglich C, Hess WR (2023) Regulation of RNase E during the UV stress response in the cyanobacterium synechocystis sp. PCC 6803. mLife 2:43–57. https://doi.org/10.1002/mlf2.12056 PubMed DOI PMC
De Weert S, Dekkers LC, Bitter W, Tuinman S, Wijfjes AHM, Van Boxtel R, Lugtenberg BJJ (2006) The two-component colR/S system of Pseudomonas fluorescens WCS365 plays a role in rhizosphere competence through maintaining the structure and function of the outer membrane. FEMS Microbiol Ecol 58:205–213. https://doi.org/10.1111/j.1574-6941.2006.00158.x PubMed DOI
Wessel AK, Yoshii Y, Reder A, Boudjemaa R, Szczesna M, Betton J-M, Bernal-Bayard J, Beloin C, Lopez D, Völker U, Ghigo J-M (2023) Escherichia coli SPFH membrane microdomain proteins HflKC contribute to aminoglycoside and oxidative stress tolerance. Microbiol Spectr. https://doi.org/10.1128/spectrum.01767-23 PubMed DOI PMC
Wong LH, Levine TP (2017) Tubular lipid binding proteins (TULIPs) growing everywhere. Biochimica et Biophysica Acta (BBA) 1864:1439–1449. https://doi.org/10.1016/j.bbamcr.2017.05.019 DOI
Xu Y, Yu W, Ma Q, Wang J, Zhou H, Jiang C (2016) The combined effect of sulfadiazine and copper on soil microbial activity and community structure. Ecotoxicol Environ Saf 134:43–52. https://doi.org/10.1016/j.ecoenv.2016.06.041 DOI
Yaganza E, Rioux D, Simard M, Arul J, Tweddell RJ (2004) Ultrastructural alterations of Erwinia carotovora subsp. atroseptica caused by treatment with aluminum chloride and sodium metabisulfite. Society 70:6800–6808. https://doi.org/10.1128/AEM.70.11.6800-6808.2004 DOI
Yamazawa, A., Takeyama, H., Takeda, D., Matsunaga, T., 1999. UV-A-induced expression of GroEL in the UVA-resistant marine cyanobacterium Oscillatoria sp. NKBG 091600. Microbiology 145, 949–954. https://doi.org/10.1099/13500872-145-4-949
Yu L, Duan H, Kellingray L, Cen S, Tian F, Zhao J, Zhang H, Gall G, Le, Mayer MJ, Zhai Q, Chen W, Narbad A (2021) Lactobacillus plantarum-mediated regulation of dietary aluminum induces changes in the human gut microbiota: an in vitro colonic fermentation study. Probiotics Antimicrob Proteins 13:398–412. https://doi.org/10.1007/s12602-020-09677-0 PubMed DOI
Zaborina O, Holbrook C, Chen Y, Long J, Zaborin A, Morozova I, Fernandez H, Wang Y, Turner JR, Alverdy JC (2008) Structure-function aspects of PstS in multi-drug-resistant Pseudomonas aeruginosa. PLoS Pathog. https://doi.org/10.1371/journal.ppat.0040043 PubMed DOI PMC
Zegers I, Martins JC, Willem R, Wyns L, Messens J (2001) Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty. Nat Struct Biol 8:843–847. https://doi.org/10.1038/nsb1001-843 PubMed DOI
Zhang M, White TA, Schuermann JP, Baban BA, Becker DF, Tanner JJ (2008) Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. Biochemistry 23:1–7
Zhang T, Shi XC, Xia Y, Mai L, Tremblay PL (2019) Escherichia coli adaptation and response to exposure to heavy atmospheric pollution. Sci Rep 9:1–13. https://doi.org/10.1038/s41598-019-47427-7 DOI
Zhao Y, Wee CY, Zhang H, Yang Z, Wang WEJ, Thian ES (2022) Silver-substituted hydroxyapatite inhibits Pseudomonas aeruginosa outer membrane protein F: a potential antibacterial mechanism. Biomater Adv 134:112713. https://doi.org/10.1016/j.msec.2022.112713 PubMed DOI
Zheng R, Feng X, Wei X, Pan X, Liu C, Song R, Jin Y, Bai F, Jin S, Wu W, Cheng Z (2018) PutA is required for virulence and regulated by PruR in Pseudomonas aeruginosa. Front Microbiol 9:1–12. https://doi.org/10.3389/fmicb.2018.00548 DOI
Zhou S, Sauvé R, Thannhauser TW (2009) Proteome changes induced by aluminium stress in tomato roots. J Exp Bot 60:1849–1857. https://doi.org/10.1093/jxb/erp065 PubMed DOI