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Volumn 8, Issue 17, 2008, Pages 3486-3493

The Ser/Thr/Tyr phosphoproteome of Lactococcus lactis IL1403 reveals multiply phosphorylated proteins

Author keywords

Kinase; Lactococcus lactis; Phosphatase; Phosphoproteome; Phosphorylation

Indexed keywords

BACTERIAL PROTEIN; PHOSPHOPEPTIDE; PHOSPHOPROTEIN; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE; PROTEOME;

EID: 52649125713     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200800069     Document Type: Article
Times cited : (131)

References (33)
  • 1
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling - 50 years and counting
    • Pawson, T., Scott, J. D., Protein phosphorylation in signaling - 50 years and counting. Trends Biochem. Sci. 2005, 30, 286-290.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 2
    • 30744464566 scopus 로고    scopus 로고
    • Ser/Thr/Tyr Protein phosphorylation in bacteria - for long time neglected, now well establised
    • Deutscher, J., Saier, M. H., Ser/Thr/Tyr Protein phosphorylation in bacteria - for long time neglected, now well establised. J. Mol. Microbiol. Biotechnol. 2005, 9, 125-131.
    • (2005) J. Mol. Microbiol. Biotechnol , vol.9 , pp. 125-131
    • Deutscher, J.1    Saier, M.H.2
  • 3
    • 0022774381 scopus 로고
    • Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis
    • Cortay, J. C., Rieul, C., Duclos, B., Cozzone, A. J., Characterization of the phosphoproteins of Escherichia coli cells by electrophoretic analysis. Eur. J. Biochem. 1986, 159, 227-237.
    • (1986) Eur. J. Biochem , vol.159 , pp. 227-237
    • Cortay, J.C.1    Rieul, C.2    Duclos, B.3    Cozzone, A.J.4
  • 4
    • 0042861585 scopus 로고    scopus 로고
    • Towards a phosphoproteome map of Corynebacterium glutamicum
    • Bendt, A. K., Burkovski, A., Schaffer, S., Bott, M. et al., Towards a phosphoproteome map of Corynebacterium glutamicum. Proteomics 2003, 3, 1637-1646.
    • (2003) Proteomics , vol.3 , pp. 1637-1646
    • Bendt, A.K.1    Burkovski, A.2    Schaffer, S.3    Bott, M.4
  • 5
    • 33645688327 scopus 로고    scopus 로고
    • Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes
    • Levine, A., Vannier, F., Absalon, C., Kuhn, L et al., Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 2006, 6, 2157-2173.
    • (2006) Proteomics , vol.6 , pp. 2157-2173
    • Levine, A.1    Vannier, F.2    Absalon, C.3    Kuhn, L.4
  • 6
    • 34648857991 scopus 로고    scopus 로고
    • Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis
    • Eymann, C., Becher, D., Bemhardt, J., Gronau, K. et al., Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 2007, 7, 3509-3526.
    • (2007) Proteomics , vol.7 , pp. 3509-3526
    • Eymann, C.1    Becher, D.2    Bemhardt, J.3    Gronau, K.4
  • 7
    • 33846683630 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: An emerging regulatory device of bacterial physiology
    • Grangeasse, C., Cozzone, A. J., Deutscher, J., Mijakovic, I., Tyrosine phosphorylation: An emerging regulatory device of bacterial physiology. Trends Biochem. Sci. 2007, 32, 86-94.
    • (2007) Trends Biochem. Sci , vol.32 , pp. 86-94
    • Grangeasse, C.1    Cozzone, A.J.2    Deutscher, J.3    Mijakovic, I.4
  • 8
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signalling networks
    • Olsen, J., Blagoy, B., Gnad, F., Macek, B. et al., Global, in vivo, and site-specific phosphorylation dynamics in signalling networks. Cell 2006, 127, 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.1    Blagoy, B.2    Gnad, F.3    Macek, B.4
  • 9
    • 34247325212 scopus 로고    scopus 로고
    • The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis
    • Macek, B., Mijakovic, I., Olsen, J. V., Gnad, F. et al., The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 2007, 6, 697-707.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 697-707
    • Macek, B.1    Mijakovic, I.2    Olsen, J.V.3    Gnad, F.4
  • 10
    • 39749166860 scopus 로고    scopus 로고
    • Phosphoproteome analysis of E.coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr Phosphorylation
    • Macek, B., Gnad, F., Soufi, B., Kumar, C. et al., Phosphoproteome analysis of E.coli reveals evolutionary conservation of bacterial Ser/Thr/Tyr Phosphorylation. Mol. Cell. Proteomics 2007, 7, 299-307.
    • (2007) Mol. Cell. Proteomics , vol.7 , pp. 299-307
    • Macek, B.1    Gnad, F.2    Soufi, B.3    Kumar, C.4
  • 11
    • 37049007689 scopus 로고    scopus 로고
    • The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: Evidence for modification by unidentified protein kinases
    • Voisin, S., Watson, D. C., Tessier, L., Ding, W. et al., The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: Evidence for modification by unidentified protein kinases. Proteomics 2007, 7, 4338-4348.
    • (2007) Proteomics , vol.7 , pp. 4338-4348
    • Voisin, S.1    Watson, D.C.2    Tessier, L.3    Ding, W.4
  • 12
    • 0035021812 scopus 로고    scopus 로고
    • The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis II-1403
    • Bolotin, A., Wincker, P., Mauger, S., Jaillon, O. et al., The complete genome sequence of the lactic acid bacterium Lactococcus lactis ssp. lactis II-1403. Genome Res. 2001, 11, 731-753.
    • (2001) Genome Res , vol.11 , pp. 731-753
    • Bolotin, A.1    Wincker, P.2    Mauger, S.3    Jaillon, O.4
  • 14
    • 0025075183 scopus 로고
    • Health and nutritional benefits from lactic acid bacteria
    • Gilliland, S. E., Health and nutritional benefits from lactic acid bacteria. FEMS Microbiol. Lett. 1990, 87, 175-188.
    • (1990) FEMS Microbiol. Lett , vol.87 , pp. 175-188
    • Gilliland, S.E.1
  • 15
    • 0034714188 scopus 로고    scopus 로고
    • Treatment of murine colitis by Lactococcus lactis secreting interleukin-10
    • Steidler, L., Hans, W., Schotte, L, Neirynck, S. et al., Treatment of murine colitis by Lactococcus lactis secreting interleukin-10. Science 2000, 289, 1352-1355.
    • (2000) Science , vol.289 , pp. 1352-1355
    • Steidler, L.1    Hans, W.2    Schotte, L.3    Neirynck, S.4
  • 16
    • 34247183123 scopus 로고    scopus 로고
    • A genomescale computational study of the interplay between transcriptional regulation and metabolism
    • Shlomi, T., Eisenberg, Y., Sharan, R., Ruppin, E., A genomescale computational study of the interplay between transcriptional regulation and metabolism. Mol. Sys. Biol. 2007, 3,101-107.
    • (2007) Mol. Sys. Biol , vol.3 , pp. 101-107
    • Shlomi, T.1    Eisenberg, Y.2    Sharan, R.3    Ruppin, E.4
  • 17
    • 18444387987 scopus 로고    scopus 로고
    • Control analysis as a tool to understand the formation of the las operon in Lactococcus lactis
    • Koebmann, B., Solem, C, Jensen, P. R., Control analysis as a tool to understand the formation of the las operon in Lactococcus lactis. FEBSJ. 2005, 272, 2292-2303.
    • (2005) FEBSJ , vol.272 , pp. 2292-2303
    • Koebmann, B.1    Solem, C.2    Jensen, P.R.3
  • 18
    • 2942562627 scopus 로고    scopus 로고
    • The phosphorylation site database: A guide to the serine-, threonine-, and/or tyrosine- phosphorylated proteins in prokaryotic organisms
    • Wurgler-Murphy, S. M., King, D. M., Kennelly, P. J., The phosphorylation site database: A guide to the serine-, threonine-, and/or tyrosine- phosphorylated proteins in prokaryotic organisms. Proteomics 2004, 4, 1562-1570.
    • (2004) Proteomics , vol.4 , pp. 1562-1570
    • Wurgler-Murphy, S.M.1    King, D.M.2    Kennelly, P.J.3
  • 19
    • 0035026054 scopus 로고    scopus 로고
    • Regulatory functions of Serine-46-phosphorylated HPr in Lactococcus lactis
    • Monedero, V., Kuipers, O. P., Jamet, E., Deutscher, J., Regulatory functions of Serine-46-phosphorylated HPr in Lactococcus lactis. J. Bacteriol. 2001, 183, 3391-3398.
    • (2001) J. Bacteriol , vol.183 , pp. 3391-3398
    • Monedero, V.1    Kuipers, O.P.2    Jamet, E.3    Deutscher, J.4
  • 20
    • 0037008092 scopus 로고    scopus 로고
    • Caught in the act: The structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis
    • Lahiri, S. D., Zhang, G., Dunaway-Mariano, D., Allen, K. N., Caught in the act: The structure of phosphorylated beta-phosphoglucomutase from Lactococcus lactis. Biochemistry 2002, 41, 8351-8359.
    • (2002) Biochemistry , vol.41 , pp. 8351-8359
    • Lahiri, S.D.1    Zhang, G.2    Dunaway-Mariano, D.3    Allen, K.N.4
  • 21
    • 0042529136 scopus 로고    scopus 로고
    • Increased exopolysaccharide production in Lactococcus lactis due to increased levels of expression of the NIZO B40 eps gene cluster
    • Boels, I. C., Van Kranenburg, R., Kanning, M. W., Chong, B. F. et al., Increased exopolysaccharide production in Lactococcus lactis due to increased levels of expression of the NIZO B40 eps gene cluster. Appl. Environ. Microbiol. 2003, 69, 5029-5031.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 5029-5031
    • Boels, I.C.1    Van Kranenburg, R.2    Kanning, M.W.3    Chong, B.F.4
  • 22
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • Olsen, J. V., de Godoy, L. M., Li, G., Macek, B. et al., Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol. Cell. Proteomics 2005, 4, 2010-2021.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.2    Li, G.3    Macek, B.4
  • 23
    • 44149105911 scopus 로고    scopus 로고
    • Management, structural and evolutionary investigation, and prediction of phosphosites
    • PHOSIDA phosphorylation site database
    • Gnad, F., Ren, S., Cox, J., Olsen, J. V. et al., PHOSIDA (phosphorylation site database): Management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 2007, 8, R250.
    • (2007) Genome Biol , vol.8
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.V.4
  • 26
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • Needleman, S. B., Wunsch, C. D., A general method applicable to the search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 1970, 48, 443-453.
    • (1970) J. Mol. Biol , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 27
    • 0034201441 scopus 로고    scopus 로고
    • The European molecular biology open software suite
    • EMBOSS
    • Rice, P., Longden, I., Bleasby, A., EMBOSS: The European molecular biology open software suite. Trends Genet. 2000, 16, 276-277.
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 28
    • 17844381893 scopus 로고    scopus 로고
    • Linear regression models for solvent accessibility prediction in proteins
    • Wagner, M., Adamczak, R., Porollo, A., Meller, J., Linear regression models for solvent accessibility prediction in proteins. J. Comput. Biol. 2005, 12, 355-369.
    • (2005) J. Comput. Biol , vol.12 , pp. 355-369
    • Wagner, M.1    Adamczak, R.2    Porollo, A.3    Meller, J.4
  • 29
    • 0038047139 scopus 로고    scopus 로고
    • Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis
    • Madec, E., Stensballe, A., Kjellström, S., Cladière, L. et al., Mass spectrometry and site-directed mutagenesis identify several autophosphorylated residues required for the activity of PrkC, a Ser/Thr kinase from Bacillus subtilis. J. Mol. Biol. 2003, 330, 459-472.
    • (2003) J. Mol. Biol , vol.330 , pp. 459-472
    • Madec, E.1    Stensballe, A.2    Kjellström, S.3    Cladière, L.4
  • 30
    • 0037344041 scopus 로고    scopus 로고
    • Proteomic analysis of Lactococcus lactis, a lactic acid bacterium
    • Guillot, A., Gitton, C., Anglade, P., Mistou, M. Y., Proteomic analysis of Lactococcus lactis, a lactic acid bacterium. Proteomics 2003, 3, 337-354.
    • (2003) Proteomics , vol.3 , pp. 337-354
    • Guillot, A.1    Gitton, C.2    Anglade, P.3    Mistou, M.Y.4
  • 31
    • 5644288462 scopus 로고    scopus 로고
    • Highly phosphorylated bacterial proteins
    • Rosen, R., Becher, D., Büttner, K., Biran, D. et al., Highly phosphorylated bacterial proteins. Proteomics 2004, 4, 3068-3077.
    • (2004) Proteomics , vol.4 , pp. 3068-3077
    • Rosen, R.1    Becher, D.2    Büttner, K.3    Biran, D.4
  • 32
    • 0037371326 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase has no control over glycolytic flux in Lactococcus lactis MG1363
    • Solem, C., Koebmann, B. J., Jensen, P. R., Glyceraldehyde-3-phosphate dehydrogenase has no control over glycolytic flux in Lactococcus lactis MG1363. J. Bacteriol. 2003, 185, 1564-1571.
    • (2003) J. Bacteriol , vol.185 , pp. 1564-1571
    • Solem, C.1    Koebmann, B.J.2    Jensen, P.R.3
  • 33
    • 33747176017 scopus 로고    scopus 로고
    • Control analysis of the importance of phosphoglycerate enolase for metabolic fluxes in Lactococcus lactis subsp. lactis IL1403
    • Koebmann, B. J., Solem, C., Jensen, P. R., Control analysis of the importance of phosphoglycerate enolase for metabolic fluxes in Lactococcus lactis subsp. lactis IL1403. IEE Proc. Syst. Biol. 2006, 153, 346-349.
    • (2006) IEE Proc. Syst. Biol , vol.153 , pp. 346-349
    • Koebmann, B.J.1    Solem, C.2    Jensen, P.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.