The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis

Av‐Gay, Yossef; Everett, Martin

doi:10.1016/s0966-842x(00)01734-0

Cited by 351 publications

(314 citation statements)

References 44 publications

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“…Although the STPKs also contain juxta-membrane phosphorylation sites implicated in regulation or binding accessory proteins (38,39), phosphorylation of the activation loop Thr is the primary mechanism of activation. Moreover, the in vitro specificity of a number of KDs has been shown to recapitulate functional substrate phosphorylations in vivo (40). Although other factors such as co-expression, co-localization, and phosphatase activity can influence functional phosphorylations in vivo, the biochemical specificity of the KDs provides a provisional network architecture.…”

Section: Stpk Intermolecular Phosphorylation Follows Specificmentioning

confidence: 99%

Biochemical and Spatial Coincidence in the Provisional Ser/Thr Protein Kinase Interaction Network of Mycobacterium tuberculosis*

Baer

Iavarone

Alber

et al. 2014

Journal of Biological Chemistry

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Background: Ser/Thr protein kinases (STPKs) form multilayered signaling networks that mediate cellular responses in eukaryotes and prokaryotes. Results: A preliminary interaction network for the STPKs in Mycobacterium tuberculosis is described. Conclusion: STPKs that cross-phosphorylate are often co-localized, suggesting multiple activation mechanisms. Significance: The initial map of this prokaryotic STPK network provides a framework for defining the logic of M. tuberculosis signaling pathways.

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Section: Stpk Intermolecular Phosphorylation Follows Specificmentioning

confidence: 99%

Biochemical and Spatial Coincidence in the Provisional Ser/Thr Protein Kinase Interaction Network of Mycobacterium tuberculosis*

Baer

Iavarone

Alber

et al. 2014

Journal of Biological Chemistry

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“…RNA polymerase sigma factors A and B were also induced, together with serine/threonine protein kinases B and G. sigB has been implicated in the M. tuberculosis response to a number of stress conditions 29 . The product of pknG is predicted to be a soluble protein (the transcription of which may be controlled by the redox status of the cell) which may be involved in glutamine uptake and which may be up-regulated under nitrogen-limiting conditions 30 . Additionally the putative nitrate/nitrite transporter narK2, the nitroreductase acg and the nitrate reductase narH were also identified to be induced.…”

Section: Microarray Data Analysismentioning

confidence: 99%

The use of microarray analysis to determine the gene expression profiles of Mycobacterium tuberculosis in response to anti-bacterial compounds

et al. 2004

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The response of Mycobacterium tuberculosis to six antimicrobial agents was determined by microarray analysis in an attempt to define mechanisms of These genes may contribute to the intrinsic resistance of M. tuberculosis to antimicrobial compounds. Further investigation into these mechanisms may elucidate novel pathways contributing to mycobacterial drug resistance and influence anti-mycobacterial drug development strategies.-3 -

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“…Two component systems, consisting of a histidine kinase with a cognate response regulator, are the most abundant signaling systems (5). Recent studies have shown that eukaryotic-type Ser/Thr protein kinases (STKs) also are present in a wide range of prokaryotic genomes and regulate complex and diverse cellular processes (6)(7)(8)(9)(10)(11)(12)(13).…”

mentioning

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.

157

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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The eukaryotic-like Ser/Thr protein kinases of Mycobacterium tuberculosis

Cited by 351 publications

References 44 publications

Biochemical and Spatial Coincidence in the Provisional Ser/Thr Protein Kinase Interaction Network of Mycobacterium tuberculosis*

Biochemical and Spatial Coincidence in the Provisional Ser/Thr Protein Kinase Interaction Network of Mycobacterium tuberculosis*

The use of microarray analysis to determine the gene expression profiles of Mycobacterium tuberculosis in response to anti-bacterial compounds

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

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