| Involvement of WalK (VicK) phosphatase activity in setting WalR (VicR) response regulator phosphorylation level and limiting cross-talk in Streptococcus pneumoniae D39 cells. | |
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MedLine Citation:
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PMID: 23013245 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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WalRK (YycFG) two-component systems (TCSs) of low-GC Gram-positive bacteria play critical roles in regulating peptidogylcan hydrolase genes involved in cell division and wall stress responses. The WalRK (VicRK) TCSs of Streptococcus pneumoniae (pneumococcus) and other Streptococcus species show numerous differences with those of other low-GC species. Notably, the pneumococcal WalK sensor kinase is not essential for normal growth in culture, unlike its homologues in Bacillus and Staphylococcus species. The WalK sensor kinase possesses histidine autokinase activity and mediates dephosphorylation of phosphorylated WalR∼P response regulator. To understand the contributions of these two WalK activities to pneumococcal growth, we constructed and characterized a set of walK kinase and phosphatase mutants in biochemical reactions and in cells. We identified an amino acid substitution in WalK that significantly reduces phosphatase activity, but not other activities. Comparisons were made between WalRK regulon expression levels and WalR∼P amounts in cells determined by Phos-tag SDS-PAGE. Reduction of WalK phosphatase activity resulted in nearly 90% phosphorylation to WalR∼P, consistent with the conclusion that WalK phosphatase is strongly active in exponentially growing cells. WalK phosphatase activity was also shown to depend on the WalK PAS domain and to limit cross-talk and the recovery of WalR∼P from walK(+) cells. |
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Authors:
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Kyle J Wayne; Shuo Li; Krystyna M Kazmierczak; Ho-Ching T Tsui; Malcolm E Winkler |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2012-09-27 |
Journal Detail:
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Title: Molecular microbiology Volume: 86 ISSN: 1365-2958 ISO Abbreviation: Mol. Microbiol. Publication Date: 2012 Nov |
Date Detail:
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Created Date: 2012-10-25 Completed Date: 2013-04-03 Revised Date: 2013-04-30 |
Medline Journal Info:
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Nlm Unique ID: 8712028 Medline TA: Mol Microbiol Country: England |
Other Details:
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Languages: eng Pagination: 645-60 Citation Subset: IM |
Copyright Information:
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© 2012 Blackwell Publishing Ltd. |
Affiliation:
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Department of Biology, Indiana University Bloomington, 1001 East Third Street, Bloomington, IN, 47405, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Bacterial Proteins
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genetics,
metabolism* Gene Expression Regulation, Bacterial* Phosphoric Monoester Hydrolases / genetics, metabolism* Phosphorylation Regulon Signal Transduction Streptococcus pneumoniae / enzymology*, genetics, growth & development, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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AI060744/AI/NIAID NIH HHS; AI095814/AI/NIAID NIH HHS; F31FM082090//PHS HHS; R01 AI060744/AI/NIAID NIH HHS; R21 AI095814/AI/NIAID NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/YycF protein, Bacteria; EC 3.1.3.-/Phosphoric Monoester Hydrolases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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