Protein phosphorylation in bacterial signal transduction

Kobir, Ahasanul; Shi, Lei; Bošković, Ana; Grangeasse, Christophe; Franjević, Damjan; Mijaković, Ivan

doi:10.1016/j.bbagen.2011.01.006

Cited by 84 publications

(72 citation statements)

References 79 publications

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“…17 Systemic studies of protein phosphorylation in bacteria commenced with the separation of phosphoproteins by 2D-gel electrophoresis. 18 Starting from 2007, high accuracy mass spectrometry in combination with biochemical enrichment of phosphopeptides from digested cell lysates lead to the publication of the first site-specific Ser/Thr/Tyr phosphoproteome for the bacterium B. subtilis. 19 The same approach has since been employed to analyze the model organisms E. coli 20 and Lactococcus lactis 21 and a number of bacterial pathogens, 22−26 and has become the standard procedure in bacterial phosphoproteomics.…”

Section: ■ Introductionmentioning

confidence: 99%

Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp. Strain PCC 7002

et al. 2013

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Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr), and tyrosine (Tyr) residues is one of the major post-translational modifications in the bacteria, involved in regulating a myriad of physiological processes. Cyanobacteria are one of the largest groups of bacteria and are the only prokaryotes capable of oxygenic photosynthesis. Many cyanobacteria strains contain unusually high numbers of protein kinases and phosphatases with specificity on Ser, Thr, and Tyr residues. However, only a few dozen phosphorylation sites in cyanobacteria are known, presenting a major obstacle for further understanding the regulatory roles of reversible phosphorylation in this group of bacteria. In this study, we carried out a global and site-specific phosphoproteomic analysis on the model cyanobacterium Synechococcus sp. PCC 7002. In total, 280 phosphopeptides and 410 phosphorylation sites from 245 Synechococcus sp. PCC 7002 proteins were identified through the combined use of protein/ peptide prefractionation, TiO 2 enrichment, and LC−MS/MS analysis. The identified phosphoproteins were functionally categorized into an interaction map and found to be involved in various biological processes such as two-component signaling pathway and photosynthesis. Our data provide the first global survey of phosphorylation in cyanobacteria by using a phosphoproteomic approach and suggest a wide-ranging regulatory scope of this modification. The provided data set may help reveal the physiological functions underlying Ser/Thr/Tyr phosphorylation and facilitate the elucidation of the entire signaling networks in cyanobacteria.

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Section: ■ Introductionmentioning

confidence: 99%

Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp. Strain PCC 7002

et al. 2013

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“…In contrast, His/Asp-based phospho-relay of two-component systems has been well recognized as a classic mode of signal transduction in the bacterial world (5). However, it wasn't until recently that eukaryotic-like Ser/Thr/Tyr phosphorylation in bacteria started to receive significant attention (6)(7)(8). Particularly, in pathogenic bacteria such as Mycobacterium tuberculosis and Staphylococcus aureus, eukaryotic-like Ser/Thr kinases (and associated phosphatases) have often been shown to participate in virulence functions (5,(9)(10)(11).…”

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confidence: 99%

Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance

Sun

Ding

et al. 2012

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

158

170

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Protein posttranslational modifications (PTMs), particularly phosphorylation, dramatically expand the complexity of cellular regulatory networks. Although cysteine (Cys) in various proteins can be subject to multiple PTMs, its phosphorylation was previously considered a rare PTM with almost no regulatory role assigned. We report here that phosphorylation occurs to a reactive cysteine residue conserved in the staphylococcal accessary regulator A (SarA)/MarR family global transcriptional regulator A (MgrA) family of proteins, and is mediated by the eukaryotic-like kinase-phosphatase pair Stk1-Stp1 in Staphylococcus aureus. Cys-phosphorylation is crucial in regulating virulence determinant production and bacterial resistance to vancomycin. Cell wall-targeting antibiotics, such as vancomycin and ceftriaxone, inhibit the kinase activity of Stk1 and lead to decreased Cys-phosphorylation of SarA and MgrA. An in vivo mouse model of infection established that the absence of stp1, which results in elevated protein Cys-phosphorylation, significantly reduces staphylococcal virulence. Our data indicate that Cys-phosphorylation is a unique PTM that can play crucial roles in bacterial signaling and regulation.

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“…A TCS typically comprises a membrane-associated sensor histidine kinase that autophosphorylates a conserved histidine residue in response to an environmental signal. This phosphate is then transferred to a conserved aspartate residue on its cognate response regulator, which alters the conformation of this protein and enhances its ability to bind to its specific recognition sequence(s) in the region of the promoter that it regulates (30). For most histidine kinases, this process is also reversible, since the histidine kinase can act as a phosphatase to remove the phosphate from the aspartate residue of its cognate response regulator.…”

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confidence: 99%

“…This regulation is accomplished by phosphorylation of protein substrates at conserved Ser and/or Thr residues (30). When the Stk substrate is an enzyme, phosphorylation may affect its activity (46,78), and when the substrate is a transcriptional regulator, phosphorylation may affect its binding to DNA (35,75), which then alters transcription of the promoters in its regulon.…”

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confidence: 99%

Serine/Threonine Protein Kinase Stk Is Required for Virulence, Stress Response, and Penicillin Tolerance in Streptococcus pyogenes

et al. 2011

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Genes encoding one or more Ser/Thr protein kinases have been identified recently in many bacteria, including one (stk) in the human pathogen Streptococcus pyogenes (group A streptococcus [GAS]). We report that in GAS, stk is required to produce disease in a murine myositis model of infection. Using microarray and quantitative reverse transcription-PCR (qRT-PCR) studies, we found that Stk activates genes for virulence factors, osmoregulation, metabolism of ␣-glucans, and fatty acid biosynthesis, as well as genes affecting cell wall synthesis. Confirming these transcription studies, we determined that the stk deletion mutant is more sensitive to osmotic stress and to penicillin than the wild type. We discuss several possible Stk phosphorylation targets that might explain Stk regulation of expression of specific operons and the possible role of Stk in resuscitation from quiescence.

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Protein phosphorylation in bacterial signal transduction

Cited by 84 publications

References 79 publications

Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp. Strain PCC 7002

Global Phosphoproteomic Analysis Reveals Diverse Functions of Serine/Threonine/Tyrosine Phosphorylation in the Model Cyanobacterium Synechococcus sp. Strain PCC 7002

Protein cysteine phosphorylation of SarA/MgrA family transcriptional regulators mediates bacterial virulence and antibiotic resistance

Serine/Threonine Protein Kinase Stk Is Required for Virulence, Stress Response, and Penicillin Tolerance in Streptococcus pyogenes

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