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PubMed

Záznam pochází z PubMed

Identification of multiple substrates of the StkP Ser/Thr protein kinase in Streptococcus pneumoniae

Journal of bacteriology. 2010 Jul ; 192 (14) : 3629-38. [epub] 20100507

J Bacteriol
ISSN 1098-5530 | 0021-9193
Zdroj

Jazyk angličtina Země Spojené státy americké Médium print-electronic

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz https://www.medvik.cz/link/pmid20453092

Online Plný text

PubMed 20453092
PubMed Central PMC2897338
DOI 10.1128/jb.01564-09
PII: JB.01564-09
Knihovny.cz E-zdroje

MeSH
bakteriální proteiny genetika metabolismus MeSH
buněčné dělení fyziologie MeSH
klonování DNA MeSH
protein-serin-threoninkinasy genetika metabolismus MeSH
regulace genové exprese enzymů fyziologie MeSH
regulace genové exprese u bakterií fyziologie MeSH
Streptococcus pneumoniae enzymologie MeSH
substrátová specifita MeSH
Publikační typ
časopisecké články MeSH
práce podpořená grantem MeSH
Názvy látek
bakteriální proteiny MeSH
protein-serin-threoninkinasy MeSH

Monitoring the external environment and responding to its changes are essential for the survival of all living organisms. The transmission of extracellular signals in prokaryotes is mediated mainly by two-component systems. In addition, genomic analyses have revealed that many bacteria contain eukaryotic-type Ser/Thr protein kinases. The human pathogen Streptococcus pneumoniae encodes 13 two-component systems and has a single copy of a eukaryotic-like Ser/Thr protein kinase gene designated stkP. Previous studies demonstrated the pleiotropic role of the transmembrane protein kinase StkP in pneumococcal physiology. StkP regulates virulence, competence, and stress resistance and plays a role in the regulation of gene expression. To determine the intracellular signaling pathways controlled by StkP, we used a proteomic approach for identification of its substrates. We detected six proteins phosphorylated on threonine by StkP continuously during growth. We identified three new substrates of StkP: the Mn-dependent inorganic pyrophosphatase PpaC, the hypothetical protein spr0334, and the cell division protein DivIVA. Contrary to the results of a previous study, we did not confirm that the alpha-subunit of RNA polymerase is a target of StkP. We showed that StkP activation and substrate recognition depend on the presence of a peptidoglycan-binding domain comprising four extracellular penicillin-binding protein- and Ser/Thr kinase-associated domain (PASTA domain) repeats. We found that StkP is regulated in a growth-dependent manner and likely senses intracellular peptidoglycan subunits present in the cell division septa. In addition, stkP inactivation results in cell division defects. Thus, the data presented here suggest that StkP plays an important role in the regulation of cell division in pneumococcus.

Cell and Molecular Microbiology Division Institute of Microbiology of the ASCR v v i Academy of Sciences of the Czech Republic Vídenská 1083 142 20 Prague 4 Czech Republic

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