ArticleMolecular microbiology2012
Involvement of WalK (VicK) phosphatase activity in setting WalR (VicR) response regulator phosphorylation level and limiting cross-talk in Streptococcus pneumoniae D39 cells.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 64 citations in OpenAlex.
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- Roles of RodZ and class A PBP1b in the assembly and regulation of the peripheral peptidoglycan elongasome in ovoid-shaped cells of Streptococcus pneumoniae D39.Molecular microbiology · 2022Article
- FabT, a Bacterial Transcriptional Repressor That Limits Futile Fatty Acid Biosynthesis.Microbiology and molecular biology reviews : MMBR · 2022Review
- Real-time detection of response regulator phosphorylation dynamics in live bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Vibrio cholerae master regulator for the activation of biofilm biogenesis genes, VpsR, senses both cyclic di-GMP and phosphate.Nucleic acids research · 2022Article
- Hybrid Histidine Kinase BinK Represses Vibrio fischeri Biofilm Signaling at Multiple Developmental Stages.Journal of bacteriology · 2021Article
- Cellular Mn/Zn Ratio Influences Phosphoglucomutase Activity and Capsule Production in Streptococcus pneumoniae D39.Journal of bacteriology · 2021Article
- Dissecting the Role of VicK Phosphatase in Aggregation and Biofilm Formation ofJournal of dental research · 2021Article
- FtsZ-Ring Regulation and Cell Division Are Mediated by Essential EzrA and Accessory Proteins ZapA and ZapJ inFrontiers in microbiology · 2021Article
- Characterization of FtsH Essentiality inFrontiers in genetics · 2021Article
- ChiS is a noncanonical DNA-binding hybrid sensor kinase that directly regulates the chitin utilization program inProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Another Breaker of the Wall: the Biological Function of the Usp45 Protein of Lactococcus lactis.Applied and environmental microbiology · 2020Article
- TheApplied and environmental microbiology · 2020Article
- The Staphylococcus aureus ArlRS two-component system regulates virulence factor expression through MgrA.Molecular microbiology · 2020Article
- Identification of an Autorepressing Two-Component Signaling System That Modulates Virulence in Streptococcus suis Serotype 2.Infection and immunity · 2019Article
- Cyclic-di-GMP binds to histidine kinase RavS to control RavS-RavR phosphotransfer and regulates the bacterial lifestyle transition between virulence and swimming.PLoS pathogens · 2019Article
- SpdC, a novel virulence factor, controls histidine kinase activity in Staphylococcus aureus.PLoS pathogens · 2018Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
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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