메뉴 건너뛰기




Volumn 13, Issue 8, 2014, Pages 1965-1978

Quantitative phosphoproteome analysis of Bacillus subtilis reveals novel substrates of the kinase PrkC and phosphatase PrpC

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; OXIDOREDUCTASE; PHOSPHATASE; PHOSPHATASE PRPC; PHOSPHOPROTEIN; PROTEIN KINASE PRKC; PROTEOME; UNCLASSIFIED DRUG; PROTEIN SERINE THREONINE KINASE; SERINE;

EID: 84905281353     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M113.035949     Document Type: Article
Times cited : (73)

References (50)
  • 1
    • 79952426399 scopus 로고    scopus 로고
    • Eukaryote-like serine/ threonine kinases and phosphatases in bacteria
    • Pereira, S. F., Goss, L., and Dworkin, J. (2011) Eukaryote-like serine/ threonine kinases and phosphatases in bacteria. Microbiol. Mol. Biol. Rev. 75, 192-212
    • (2011) Microbiol. Mol. Biol. Rev. , vol.75 , pp. 192-212
    • Pereira, S.F.1    Goss, L.2    Dworkin, J.3
  • 2
    • 84862596522 scopus 로고    scopus 로고
    • Impact of phosphoproteomics on studies of bacterial physiology
    • Mijakovic, I., and Macek, B. (2012) Impact of phosphoproteomics on studies of bacterial physiology. FEMS Microbiol. Rev. 36, 877-892
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 877-892
    • Mijakovic, I.1    Macek, B.2
  • 3
    • 0037384743 scopus 로고    scopus 로고
    • Phosphorylation-mediated regulation of heat shock response in Escherichia coli
    • DOI 10.1046/j.1365-2958.2003.03449.x
    • Klein, G., Dartigalongue, C., and Raina, S. (2003) Phosphorylation- mediated regulation of heat shock response in Escherichia coli. Mol. Microbiol. 48, 269-285 (Pubitemid 36411482)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 269-285
    • Klein, G.1    Dartigalongue, C.2    Raina, S.3
  • 4
    • 80052336731 scopus 로고    scopus 로고
    • An essential tyrosine phosphatase homolog regulates cell separation, outer membrane integrity, and morphology in Caulobacter crescentus
    • Shapland, E. B., Reisinger, S. J., Bajwa, A. K., and Ryan, K. R. (2011) An essential tyrosine phosphatase homolog regulates cell separation, outer membrane integrity, and morphology in Caulobacter crescentus. J. Bacteriol. 193, 4361-4370
    • (2011) J. Bacteriol. , vol.193 , pp. 4361-4370
    • Shapland, E.B.1    Reisinger, S.J.2    Bajwa, A.K.3    Ryan, K.R.4
  • 5
    • 30744478198 scopus 로고    scopus 로고
    • Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens
    • Cozzone, A. J. (2005) Role of protein phosphorylation on serine/threonine and tyrosine in the virulence of bacterial pathogens. J. Mol. Microbiol. Biotechnol. 9, 198-213
    • (2005) J. Mol. Microbiol. Biotechnol. , vol.9 , pp. 198-213
    • Cozzone, A.J.1
  • 6
    • 0028917215 scopus 로고
    • Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in gram-positive bacteria
    • Deutscher, J., Kuster, E., Bergstedt, U., Charrier, V., and Hillen, W. (1995) Protein kinase-dependent HPr/CcpA interaction links glycolytic activity to carbon catabolite repression in gram-positive bacteria. Mol. Microbiol. 15, 1049-1053
    • (1995) Mol. Microbiol. , vol.15 , pp. 1049-1053
    • Deutscher, J.1    Kuster, E.2    Bergstedt, U.3    Charrier, V.4    Hillen, W.5
  • 7
    • 84878392320 scopus 로고    scopus 로고
    • Bacillus subtilis serine/threonine protein kinase YabT is involved in spore development via phosphorylation of a bacterial recombinase
    • Bidnenko, V., Shi, L., Kobir, A., Ventroux, M., Pigeonneau, N., Henry, C., Trubuil, A., Noirot-Gros, M. F., and Mijakovic, I. (2013) Bacillus subtilis serine/threonine protein kinase YabT is involved in spore development via phosphorylation of a bacterial recombinase. Mol. Microbiol. 88, 921-935
    • (2013) Mol. Microbiol. , vol.88 , pp. 921-935
    • Bidnenko, V.1    Shi, L.2    Kobir, A.3    Ventroux, M.4    Pigeonneau, N.5    Henry, C.6    Trubuil, A.7    Noirot-Gros, M.F.8    Mijakovic, I.9
  • 8
    • 54549099189 scopus 로고    scopus 로고
    • A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments
    • Shah, I. M., Laaberki, M. H., Popham, D. L., and Dworkin, J. (2008) A eukaryotic-like Ser/Thr kinase signals bacteria to exit dormancy in response to peptidoglycan fragments. Cell 135, 486-496
    • (2008) Cell , vol.135 , pp. 486-496
    • Shah, I.M.1    Laaberki, M.H.2    Popham, D.L.3    Dworkin, J.4
  • 9
    • 0006039719 scopus 로고    scopus 로고
    • Homologous pairs of regulatory proteins control activity of Bacillus subtilis transcription factor sigma(B) in response to environmental stress
    • Kang, C. M., Brody, M. S., Akbar, S., Yang, X., and Price, C. W. (1996) Homologous pairs of regulatory proteins control activity of Bacillus subtilis transcription factor sigma(b) in response to environmental stress. J. Bacteriol. 178, 3846-3853 (Pubitemid 26227201)
    • (1996) Journal of Bacteriology , vol.178 , Issue.13 , pp. 3846-3853
    • Kang, C.M.1    Brody, M.S.2    Akbar, S.3    Yang, X.4    Price, C.W.5
  • 10
    • 79751501463 scopus 로고    scopus 로고
    • Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain
    • Jers, C., Kobir, A., Sondergaard, E. O., Jensen, P. R., and Mijakovic, I. (2011) Bacillus subtilis two-component system sensory kinase DegS is regulated by serine phosphorylation in its input domain. PLoS One 6, e14653
    • (2011) PLoS One , vol.6
    • Jers, C.1    Kobir, A.2    Sondergaard, E.O.3    Jensen, P.R.4    Mijakovic, I.5
  • 12
    • 33947263138 scopus 로고    scopus 로고
    • Bacillus subtilis strain deficient for the protein-tyrosine kinase PtkA exhibits impaired DNA replication
    • DOI 10.1111/j.1365-2958.2007.05625.x
    • Petranovic, D., Michelsen, O., Zahradka, K., Silva, C., Petranovic, M., Jensen, P. R., and Mijakovic, I. (2007) Bacillus subtilis strain deficient for the protein-tyrosine kinase PtkA exhibits impaired DNA replication. Mol. Microbiol. 63, 1797-1805 (Pubitemid 46426704)
    • (2007) Molecular Microbiology , vol.63 , Issue.6 , pp. 1797-1805
    • Petranovic, D.1    Michelsen, O.2    Zahradka, K.3    Silva, C.4    Petranovic, M.5    Jensen, P.R.6    Mijakovic, I.7
  • 15
    • 0036428610 scopus 로고    scopus 로고
    • Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes
    • DOI 10.1046/j.1365-2958.2002.03178.x
    • Madec, E., Laszkiewicz, A., Iwanicki, A., Obuchowski, M., and Seror, S. (2002) Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes. Mol. Microbiol. 46, 571-586 (Pubitemid 35340965)
    • (2002) Molecular Microbiology , vol.46 , Issue.2 , pp. 571-586
    • Madec, E.1    Laszkiewicz, A.2    Iwanicki, A.3    Obuchowski, M.4    Seror, S.5
  • 16
    • 0036842045 scopus 로고    scopus 로고
    • The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells
    • DOI 10.1128/JB.184.22.6109-6114.2002
    • Gaidenko, T. A., Kim, T. J., and Price, C. W. (2002) The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells. J. Bacteriol. 184, 6109-6114 (Pubitemid 35265890)
    • (2002) Journal of Bacteriology , vol.184 , Issue.22 , pp. 6109-6114
    • Gaidenko, T.A.1    Kim, T.-J.2    Price, C.W.3
  • 17
    • 77950616042 scopus 로고    scopus 로고
    • In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism
    • Pietack, N., Becher, D., Schmidl, S. R., Saier, M. H., Hecker, M., Commichau, F. M., and Stulke, J. (2010) In vitro phosphorylation of key metabolic enzymes from Bacillus subtilis: PrkC phosphorylates enzymes from different branches of basic metabolism. J. Mol. Microbiol. Biotechnol. 18, 129-140
    • (2010) J. Mol. Microbiol. Biotechnol. , vol.18 , pp. 129-140
    • Pietack, N.1    Becher, D.2    Schmidl, S.R.3    Saier, M.H.4    Hecker, M.5    Commichau, F.M.6    Stulke, J.7
  • 18
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation
    • DOI 10.1074/mcp.M700311-MCP200
    • Macek, B., Gnad, F., Soufi, B., Kumar, C., Olsen, J. V., Mijakovic, I., and Mann, M. (2008) Phosphoproteome analysis of E. coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr phosphorylation. Mol. Cell. Proteomics 7, 299-307 (Pubitemid 351298444)
    • (2008) Molecular and Cellular Proteomics , vol.7 , Issue.2 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4    Olsen, J.V.5    Mijakovic, I.6    Mann, M.7
  • 19
    • 52649125713 scopus 로고    scopus 로고
    • The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins
    • Soufi, B., Gnad, F., Jensen, P. R., Petranovic, D., Mann, M., Mijakovic, I., and Macek, B. (2008) The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins. Proteomics 8, 3486-3493
    • (2008) Proteomics , vol.8 , pp. 3486-3493
    • Soufi, B.1    Gnad, F.2    Jensen, P.R.3    Petranovic, D.4    Mann, M.5    Mijakovic, I.6    Macek, B.7
  • 20
    • 66449094321 scopus 로고    scopus 로고
    • Ser/Thr/Tyr phosphoproteome analysis of pathogenic and nonpathogenic Pseudomonas species
    • Ravichandran, A., Sugiyama, N., Tomita, M., Swarup, S., and Ishihama, Y. (2009) Ser/Thr/Tyr phosphoproteome analysis of pathogenic and nonpathogenic Pseudomonas species. Proteomics 9, 2764-2775
    • (2009) Proteomics , vol.9 , pp. 2764-2775
    • Ravichandran, A.1    Sugiyama, N.2    Tomita, M.3    Swarup, S.4    Ishihama, Y.5
  • 23
    • 34648857991 scopus 로고    scopus 로고
    • Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis
    • DOI 10.1002/pmic.200700232
    • Eymann, C., Becher, D., Bernhardt, J., Gronau, K., Klutzny, A., and Hecker, M. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7, 3509-3526 (Pubitemid 47597674)
    • (2007) Proteomics , vol.7 , Issue.19 , pp. 3509-3526
    • Eymann, C.1    Becher, D.2    Bernhardt, J.3    Gronau, K.4    Klutzny, A.5    Hecker, M.6
  • 24
    • 34247325212 scopus 로고    scopus 로고
    • The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis
    • DOI 10.1074/mcp.M600464-MCP200
    • Macek, B., Mijakovic, I., Olsen, J. V., Gnad, F., Kumar, C., Jensen, P. R., and Mann, M. (2007) The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6, 697-707 (Pubitemid 46630102)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.4 , pp. 697-707
    • Macek, B.1    Mijakovic, I.2    Olsen, J.V.3    Gnad, F.4    Kumar, C.5    Jensen, P.R.6    Mann, M.7
  • 25
    • 77954371891 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis
    • Soufi, B., Kumar, C., Gnad, F., Mann, M., Mijakovic, I., and Macek, B. (2010) Stable isotope labeling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Bacillus subtilis. J. Proteome Res. 9, 3638-3646
    • (2010) J. Proteome Res. , vol.9 , pp. 3638-3646
    • Soufi, B.1    Kumar, C.2    Gnad, F.3    Mann, M.4    Mijakovic, I.5    Macek, B.6
  • 27
    • 0030027865 scopus 로고    scopus 로고
    • Efficient insertional mutagenesis in lactococci and other gram-positive bacteria
    • Maguin, E., Prevost, H., Ehrlich, S. D., and Gruss, A. (1996) Efficient insertional mutagenesis in lactococci and other gram-positive bacteria. J. Bacteriol. 178, 931-935 (Pubitemid 26036674)
    • (1996) Journal of Bacteriology , vol.178 , Issue.3 , pp. 931-935
    • Maguin, E.1    Prevost, H.2    Ehrlich, S.D.3    Gruss, A.4
  • 28
    • 0035026054 scopus 로고    scopus 로고
    • Regulatory functions of serine-46-phosphorylated HPr in Lactococcus lactis
    • DOI 10.1128/JB.183.11.3391-3398.2001
    • Monedero, V., Kuipers, O. P., Jamet, E., and Deutscher, J. (2001) Regulatory functions of serine-46-phosphorylated HPr in Lactococcus lactis. J. Bacteriol. 183, 3391-3398 (Pubitemid 32448603)
    • (2001) Journal of Bacteriology , vol.183 , Issue.11 , pp. 3391-3398
    • Monedero, V.1    Kuipers, O.P.2    Jamet, E.3    Deutscher, J.4
  • 29
    • 0001639179 scopus 로고
    • The Growth of Bacterial Cultures
    • Monod, J. (1949) The Growth of Bacterial Cultures. Ann. Rev. Microbiol. 3, 371-394
    • (1949) Ann. Rev. Microbiol. , vol.3 , pp. 371-394
    • Monod, J.1
  • 30
    • 33645774852 scopus 로고    scopus 로고
    • Modular stop and go extraction tips with stacked disks for parallel and multidimensional Peptide fractionation in proteomics
    • Ishihama, Y., Rappsilber, J., and Mann, M. (2006) Modular stop and go extraction tips with stacked disks for parallel and multidimensional Peptide fractionation in proteomics. J. Proteome Res. 5, 988-994
    • (2006) J. Proteome Res. , vol.5 , pp. 988-994
    • Ishihama, Y.1    Rappsilber, J.2    Mann, M.3
  • 32
    • 84887111113 scopus 로고    scopus 로고
    • Deep coverage of the Escherichia coli proteome enables the assessment of false discovery rates in simple proteogenomic experiments
    • Krug, K., Carpy, A., Behrends, G., Matic, K., Soares, N. C., and Macek, B. (2013) Deep coverage of the Escherichia coli proteome enables the assessment of false discovery rates in simple proteogenomic experiments. Mol. Cell. Proteomics
    • (2013) Mol. Cell. Proteomics
    • Krug, K.1    Carpy, A.2    Behrends, G.3    Matic, K.4    Soares, N.C.5    Macek, B.6
  • 34
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox, J., Matic, I., Hilger, M., Nagaraj, N., Selbach, M., Olsen, J. V., and Mann, M. (2009) A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4, 698-705
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 37
    • 0001677717 scopus 로고
    • Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing
    • Benjamini, Y., and Hochberg, Y. (1995) Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing. J. Roy. Statistical Soc. Series B 57, 289-300
    • (1995) J. Roy. Statistical Soc. Series B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 38
    • 77949285003 scopus 로고    scopus 로고
    • The catalytic property of 3-hydroxyisobutyrate dehydrogenase from Bacillus cereus on 3-hydroxypropionate
    • Yao, T., Xu, L., Ying, H., Huang, H., and Yan, M. (2010) The catalytic property of 3-hydroxyisobutyrate dehydrogenase from Bacillus cereus on 3-hydroxypropionate. Appl. Biochem. Biotechnol. 160, 694-703
    • (2010) Appl. Biochem. Biotechnol. , vol.160 , pp. 694-703
    • Yao, T.1    Xu, L.2    Ying, H.3    Huang, H.4    Yan, M.5
  • 39
    • 84879401680 scopus 로고    scopus 로고
    • Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium
    • Soares, N. C., Spat, P., Krug, K., and Macek, B. (2013) Global dynamics of the Escherichia coli proteome and phosphoproteome during growth in minimal medium. J. Proteome Res. 12, 2611-2621
    • (2013) J. Proteome Res. , vol.12 , pp. 2611-2621
    • Soares, N.C.1    Spat, P.2    Krug, K.3    Macek, B.4
  • 40
    • 75149130051 scopus 로고    scopus 로고
    • Targeting the cancer kinome through polypharmacology
    • Knight, Z. A., Lin, H., and Shokat, K. M. (2010) Targeting the cancer kinome through polypharmacology. Nat. Rev. Cancer 10, 130-137
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 130-137
    • Knight, Z.A.1    Lin, H.2    Shokat, K.M.3
  • 41
    • 0030199542 scopus 로고    scopus 로고
    • Strong control on the transit time in metabolic channelling
    • DOI 10.1016/0014-5793(96)00532-7
    • Kholodenko, B. N., Sakamoto, N., Puigjaner, J., Westerhoff, H. V., and Cascante, M. (1996) Strong control on the transit time in metabolic channelling. FEBS Lett. 389, 123-125 (Pubitemid 26226483)
    • (1996) FEBS Letters , vol.389 , Issue.2 , pp. 123-125
    • Kholodenko, B.N.1    Sakamoto, N.2    Puigjaner, J.3    Westerhoff, H.V.4    Cascante, M.5
  • 43
    • 0028929877 scopus 로고
    • Differential expression of two closely related deoxyribonuclease genes, nucA and nucB, in Bacillus subtilis
    • van Sinderen, D., Kiewiet, R., and Venema, G. (1995) Differential expression of two closely related deoxyribonuclease genes, nucA and nucB, in Bacillus subtilis. Mol. Microbiol. 15, 213-223
    • (1995) Mol. Microbiol. , vol.15 , pp. 213-223
    • Van Sinderen, D.1    Kiewiet, R.2    Venema, G.3
  • 44
    • 51549089016 scopus 로고    scopus 로고
    • Molecular mechanisms underlying the positive stringent response of the Bacillus subtilis ilv-leu operon, involved in the biosynthesis of branched-chain amino acids
    • Tojo, S., Satomura, T., Kumamoto, K., Hirooka, K., and Fujita, Y. (2008) Molecular mechanisms underlying the positive stringent response of the Bacillus subtilis ilv-leu operon, involved in the biosynthesis of branched-chain amino acids. J. Bacteriol. 190, 6134-6147
    • (2008) J. Bacteriol. , vol.190 , pp. 6134-6147
    • Tojo, S.1    Satomura, T.2    Kumamoto, K.3    Hirooka, K.4    Fujita, Y.5
  • 45
    • 0030895003 scopus 로고    scopus 로고
    • The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the Pho regulon
    • Qi, Y., Kobayashi, Y., and Hulett, F. M. (1997) The pst operon of Bacillus subtilis has a phosphate-regulated promoter and is involved in phosphate transport but not in regulation of the pho regulon. J. Bacteriol. 179, 2534-2539 (Pubitemid 27164551)
    • (1997) Journal of Bacteriology , vol.179 , Issue.8 , pp. 2534-2539
    • Qi, Y.1    Kobayashi, Y.2    Hulett, F.M.3
  • 46
    • 0033895238 scopus 로고    scopus 로고
    • Phosphate starvation-inducible proteins of Bacillus subtilis: Proteomics and transcriptional analysis
    • DOI 10.1128/JB.182.16.4478-4490.2000
    • Antelmann, H., Scharf, C., and Hecker, M. (2000) Phosphate starvation-inducible proteins of Bacillus subtilis: proteomics and transcriptional analysis. J. Bacteriol. 182, 4478-4490 (Pubitemid 30599811)
    • (2000) Journal of Bacteriology , vol.182 , Issue.16 , pp. 4478-4490
    • Antelmann, H.1    Scharf, C.2    Hecker, M.3
  • 48
    • 33645056701 scopus 로고    scopus 로고
    • Targets of the master regulator of biofilm formation in Bacillus subtilis
    • Chu, F., Kearns, D. B., Branda, S. S., Kolter, R., and Losick, R. (2006) Targets of the master regulator of biofilm formation in Bacillus subtilis. Mol. Microbiol. 59, 1216-1228
    • (2006) Mol. Microbiol. , vol.59 , pp. 1216-1228
    • Chu, F.1    Kearns, D.B.2    Branda, S.S.3    Kolter, R.4    Losick, R.5
  • 49
    • 0031033042 scopus 로고    scopus 로고
    • Expression of AbrB, a transition state regulator from Bacillus subtilis, is growth phase dependent in a manner resembling that of Fis, the nucleoid binding protein from Escherichia coli
    • O'Reilly, M., and Devine, K. M. (1997) Expression of AbrB, a transition state regulator from Bacillus subtilis, is growth phase dependent in a manner resembling that of Fis, the nucleoid binding protein from Escherichia coli. J. Bacteriol. 179, 522-529 (Pubitemid 27030407)
    • (1997) Journal of Bacteriology , vol.179 , Issue.2 , pp. 522-529
    • O'Reilly, M.1    Devine, K.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.