• Je něco špatně v tomto záznamu ?

OsmC and incomplete glycine decarboxylase complex mediate reductive detoxification of peroxides in hydrogenosomes of Trichomonas vaginalis

E. Nývltová, T. Smutná, J. Tachezy, I. Hrdý,

. 2016 ; 206 (1-2) : 29-38. [pub] 20160118

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc17031867

Osmotically inducible protein (OsmC) and organic hydroperoxide resistance protein (Ohr) are small, thiol-dependent peroxidases that comprise a family of prokaryotic protective proteins central to the defense against deleterious effects of organic hydroperoxides, which are reactive molecules that are formed during interactions between the host immune system and pathogens. Trichomonas vaginalis, a sexually transmitted parasite of humans, possesses OsmC homologues in its hydrogenosomes, anaerobic mitochondrial organelles that harbor enzymes and pathways that are sensitive to oxidative damage. The glycine decarboxylase complex (GDC), which consists of four proteins (i.e., L, H, P and T), is in eukaryotes exclusively mitochondrial enzymatic system that catalyzes oxidative decarboxylation and deamination of glycine. However, trichomonad hydrogenosomes contain only the L and H proteins, whose physiological functions are unknown. Here, we found that the hydrogenosomal L and H proteins constitute a lipoate-dependent redox system that delivers electrons from reduced nicotinamide adenine dinucleotide (NADH) to OsmC for the reductive detoxification of peroxides. Our searches of genome databases revealed that, in addition to prokaryotes, homologues of OsmC/Ohr family proteins with predicted mitochondrial localization are present in various eukaryotic lineages. Therefore, we propose that the novel OsmC-GDC-based redox system may not be limited to T. vaginalis.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc17031867
003      
CZ-PrNML
005      
20171102113204.0
007      
ta
008      
171025s2016 ne f 000 0|eng||
009      
AR
024    7_
$a 10.1016/j.molbiopara.2016.01.006 $2 doi
035    __
$a (PubMed)26794804
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a ne
100    1_
$a Nývltová, Eva $u Department of Parasitology, Charles University in Prague, Faculty of Science, Prague, Czech Republic.
245    10
$a OsmC and incomplete glycine decarboxylase complex mediate reductive detoxification of peroxides in hydrogenosomes of Trichomonas vaginalis / $c E. Nývltová, T. Smutná, J. Tachezy, I. Hrdý,
520    9_
$a Osmotically inducible protein (OsmC) and organic hydroperoxide resistance protein (Ohr) are small, thiol-dependent peroxidases that comprise a family of prokaryotic protective proteins central to the defense against deleterious effects of organic hydroperoxides, which are reactive molecules that are formed during interactions between the host immune system and pathogens. Trichomonas vaginalis, a sexually transmitted parasite of humans, possesses OsmC homologues in its hydrogenosomes, anaerobic mitochondrial organelles that harbor enzymes and pathways that are sensitive to oxidative damage. The glycine decarboxylase complex (GDC), which consists of four proteins (i.e., L, H, P and T), is in eukaryotes exclusively mitochondrial enzymatic system that catalyzes oxidative decarboxylation and deamination of glycine. However, trichomonad hydrogenosomes contain only the L and H proteins, whose physiological functions are unknown. Here, we found that the hydrogenosomal L and H proteins constitute a lipoate-dependent redox system that delivers electrons from reduced nicotinamide adenine dinucleotide (NADH) to OsmC for the reductive detoxification of peroxides. Our searches of genome databases revealed that, in addition to prokaryotes, homologues of OsmC/Ohr family proteins with predicted mitochondrial localization are present in various eukaryotic lineages. Therefore, we propose that the novel OsmC-GDC-based redox system may not be limited to T. vaginalis.
650    _2
$a sekvence aminokyselin $7 D000595
650    _2
$a axenická kultura $7 D061245
650    _2
$a klonování DNA $7 D003001
650    _2
$a Escherichia coli $x genetika $x metabolismus $7 D004926
650    _2
$a exprese genu $7 D015870
650    _2
$a systém štěpení glycinu $x genetika $x metabolismus $7 D050959
650    _2
$a peroxid vodíku $x metabolismus $7 D006861
650    _2
$a kinetika $7 D007700
650    _2
$a I. fáze biotransformace $x genetika $7 D050216
650    _2
$a mitochondrie $x metabolismus $x ultrastruktura $7 D008928
650    _2
$a oxidace-redukce $7 D010084
650    _2
$a peroxidasy $x genetika $x metabolismus $7 D010544
650    _2
$a fylogeneze $7 D010802
650    _2
$a vazba proteinů $7 D011485
650    _2
$a protozoální proteiny $x genetika $x metabolismus $7 D015800
650    _2
$a rekombinantní proteiny $x genetika $x metabolismus $7 D011994
650    _2
$a sekvenční seřazení $7 D016415
650    _2
$a sekvenční homologie aminokyselin $7 D017386
650    _2
$a Trichomonas vaginalis $x genetika $x metabolismus $x ultrastruktura $7 D014246
655    _2
$a časopisecké články $7 D016428
700    1_
$a Smutná, Tamara $u Department of Parasitology, Charles University in Prague, Faculty of Science, Prague, Czech Republic.
700    1_
$a Tachezy, Jan $u Department of Parasitology, Charles University in Prague, Faculty of Science, Prague, Czech Republic.
700    1_
$a Hrdý, Ivan $u Department of Parasitology, Charles University in Prague, Faculty of Science, Prague, Czech Republic. Electronic address: hrdy@cesnet.cz.
773    0_
$w MED00003384 $t Molecular and biochemical parasitology $x 1872-9428 $g Roč. 206, č. 1-2 (2016), s. 29-38
856    41
$u https://pubmed.ncbi.nlm.nih.gov/26794804 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20171025 $b ABA008
991    __
$a 20171102113257 $b ABA008
999    __
$a ok $b bmc $g 1255460 $s 992894
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2016 $b 206 $c 1-2 $d 29-38 $e 20160118 $i 1872-9428 $m Molecular and biochemical parasitology $n Mol Biochem Parasitol $x MED00003384
LZP    __
$a Pubmed-20171025

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...