Article: article from journal or magazin.
Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP.
Proceedings of the National Academy of Sciences of the United States of America
How the human pathogen Streptococcus pneumoniae coordinates cell-wall synthesis during growth and division to achieve its characteristic oval shape is poorly understood. The conserved eukaryotic-type Ser/Thr kinase of S. pneumoniae, StkP, previously was reported to phosphorylate the cell-division protein DivIVA. Consistent with a role in cell division, GFP-StkP and its cognate phosphatase, GFP-PhpP, both localize to the division site. StkP localization depends on its penicillin-binding protein and Ser/Thr-associated domains that likely sense uncross-linked peptidoglycan, because StkP and PhpP delocalize in the presence of antibiotics that target the latest stages of cell-wall biosynthesis and in cells that have stopped dividing. Time-lapse microscopy shows that StkP displays an intermediate timing of recruitment to midcell: StkP arrives shortly after FtsA but before DivIVA. Furthermore, StkP remains at midcell longer than FtsA, until division is complete. Cells mutated for stkP are perturbed in cell-wall synthesis and display elongated morphologies with multiple, often unconstricted, FtsA and DivIVA rings. The data show that StkP plays an important role in regulating cell-wall synthesis and controls correct septum progression and closure. Overall, our results indicate that StkP signals information about the cell-wall status to key cell-division proteins and in this way acts as a regulator of cell division.
Anti-Bacterial Agents/pharmacology, Bacterial Proteins/chemistry, Bacterial Proteins/metabolism, Cell Division/drug effects, Cell Proliferation/drug effects, Cell Wall/drug effects, Cell Wall/metabolism, Conserved Sequence, Enzyme Activation/drug effects, Extracellular Space/drug effects, Extracellular Space/metabolism, Green Fluorescent Proteins/metabolism, Humans, Ligands, Models, Biological, Phosphorylation/drug effects, Protein Structure, Tertiary, Protein Transport/drug effects, Protein-Serine-Threonine Kinases/chemistry, Protein-Serine-Threonine Kinases/metabolism, Recombinant Fusion Proteins/metabolism, Streptococcus pneumoniae/cytology, Streptococcus pneumoniae/drug effects, Time Factors
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