Genetic and biochemical analysis of the serine/threonine protein kinases PknA, PknB, PknG and PknL of <i>Corynebacterium glutamicum</i>: evidence for non‐essentiality and for phosphorylation of OdhI and FtsZ by multiple kinases

Schultz, Christian; Niebisch, Axel; Schwaiger, Astrid; Viets, Ulrike; Metzger, Sabine; Bramkamp, Marc; Bott, Michael

doi:10.1111/j.1365-2958.2009.06897.x

Cited by 85 publications

(73 citation statements)

References 39 publications

(125 reference statements)

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“…In previous reports, we have characterized the four STPKs of C. glutamicum and demonstrated that the PknA and PknB kinases were involved in cell division and PG biosynthesis. Moreover, different STPK substrates have been identified and characterized as proteins involved in cell division and PG biosynthesis thus confirming the critical role of Ser/Thr phosphorylation in regulating such pathways (34,62). Therefore, we hypothesized that RsmP could be regulated via STPK phosphorylation, and this was confirmed in this study by evidence that corynebacterial PknA and PknL can phosphorylate RsmP.…”

Section: Discussionsupporting

confidence: 69%

Phosphorylation of a Novel Cytoskeletal Protein (RsmP) Regulates Rod-shaped Morphology in Corynebacterium glutamicum

Fiuza

Letek

Leiba

et al. 2010

Journal of Biological Chemistry

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Corynebacteria grow by wall extension at the cell poles, with DivIVA being an essential protein orchestrating cell elongation and morphogenesis. DivIVA is considered a scaffolding protein able to recruit other proteins and enzymes involved in polar peptidoglycan biosynthesis. Partial depletion of DivIVA induced overexpression of cg3264, a previously uncharacterized gene that encodes a novel coiled coil-rich protein specific for corynebacteria and a few other actinomycetes. By partial depletion and overexpression of Cg3264, we demonstrated that this protein is an essential cytoskeletal element needed for maintenance of the rod-shaped morphology of Corynebacterium glutamicum, and it was therefore renamed RsmP (rod-shaped morphology protein). RsmP forms long polymers in vitro in the absence of any cofactors, thus resembling eukaryotic intermediate filaments. We also investigated whether RsmP could be regulated post-translationally by phosphorylation, like eukaryotic intermediate filaments. RsmP was phosphorylated in vitro by the PknA protein kinase and to a lesser extent by PknL. A mass spectrometric analysis indicated that phosphorylation exclusively occurred on a serine (Ser-6) and two threonine (Thr-168 and Thr-211) residues. We confirmed that mutagenesis to alanine (phosphoablative protein) totally abolished PknA-dependent phosphorylation of RsmP. Interestingly, when the three residues were converted to aspartic acid, the phosphomimetic protein accumulated at the cell poles instead of making filaments along the cell, as observed for the native or phosphoablative RsmP proteins, indicating that phosphorylation of RsmP is necessary for directing cell growth at the cell poles.

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Section: Discussionsupporting

confidence: 69%

Phosphorylation of a Novel Cytoskeletal Protein (RsmP) Regulates Rod-shaped Morphology in Corynebacterium glutamicum

Fiuza

Letek

Leiba

et al. 2010

Journal of Biological Chemistry

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“…For instance, although StkP efficiently phosphorylates FtsZ in vitro, negligible (if any) differences in phosphorylation patterns were observed using anti-pThr antibodies after immunoprecipitation in stkP mutants (34). However, FtsZ also was shown to be phosphorylated in Corynebacterium glutamicum, Streptomyces coelicolor, and Streptococcus agalactiae (20,51,52), suggesting that STK-dependent phosphorylation of FtsZ is widespread in Gram-positive bacteria.…”

Section: Discussionmentioning

confidence: 99%

Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP

Beilharz

Novaková

Fadda

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

153

276

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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.

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“…While eSTKs regulate many essential bacterial processes, most eSTKs are not themselves essential, with M. tuberculosis PknA and PknB being prominent exceptions (47,75,150). The reported essentiality of the C. glutamicum PknA and PknB homologs appears to be strain specific (49,157). While mutations in B. subtilis PrkC (50,159) or in the eSTKs of several streptococcal species (68,72,144) revealed that these proteins are not, strictly speaking, essential, they led to significant stationary-phase survival defects.…”

Section: Estks In Bacteriamentioning

confidence: 99%

Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

Pereira

Goss

Dworkin

2011

Microbiol Mol Biol Rev

316

348

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SUMMARY Genomic studies have revealed the presence of Ser/Thr kinases and phosphatases in many bacterial species, although their physiological roles have largely been unclear. Here we review bacterial Ser/Thr kinases (eSTKs) that show homology in their catalytic domains to eukaryotic Ser/Thr kinases and their partner phosphatases (eSTPs) that are homologous to eukaryotic phosphatases. We first discuss insights into the enzymatic mechanism of eSTK activation derived from structural studies on both the ligand-binding and catalytic domains. We then turn our attention to the identified substrates of eSTKs and eSTPs for a number of species and to the implications of these findings for understanding their physiological roles in these organisms.

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Genetic and biochemical analysis of the serine/threonine protein kinases PknA, PknB, PknG and PknL of Corynebacterium glutamicum: evidence for non‐essentiality and for phosphorylation of OdhI and FtsZ by multiple kinases

Cited by 85 publications

References 39 publications

Phosphorylation of a Novel Cytoskeletal Protein (RsmP) Regulates Rod-shaped Morphology in Corynebacterium glutamicum

Phosphorylation of a Novel Cytoskeletal Protein (RsmP) Regulates Rod-shaped Morphology in Corynebacterium glutamicum

Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP

Eukaryote-Like Serine/Threonine Kinases and Phosphatases in Bacteria

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