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Volumn 56, Issue 2, 2005, Pages 383-396

Translation elongation factor EF-Tu is a target for Stp, a serine-threonine phosphatase involved in virulence of Listeria monocytogenes

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR TU; MANGANESE; MOCIMYCIN; PHOSPHATASE; PROTEIN SERINE THREONINE KINASE; SERINE THREONINE PHOSPHATASE STP; TRANSFER RNA; TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 17144424245     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04551.x     Document Type: Article
Times cited : (90)

References (57)
  • 2
    • 8744309111 scopus 로고    scopus 로고
    • New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, Gram-positive bacteria
    • Arnaud, M., Chastanet, A., and Debarbouille, M. (2004) New vector for efficient allelic replacement in naturally nontransformable, low-GC-content, Gram-positive bacteria. Appl Environ Microbiol 70: 6887-6891.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6887-6891
    • Arnaud, M.1    Chastanet, A.2    Debarbouille, M.3
  • 3
    • 0031860103 scopus 로고    scopus 로고
    • The structure and mechanism of protein phosphatases: Insights into catalysis and regulation
    • Barford, D., Das, A.K., and Egloff, M.P. (1998) The structure and mechanism of protein phosphatases: insights into catalysis and regulation. Annu Rev Biophys Biomol Struct 27: 133-164.
    • (1998) Annu Rev Biophys Biomol Struct , vol.27 , pp. 133-164
    • Barford, D.1    Das, A.K.2    Egloff, M.P.3
  • 4
    • 0029954661 scopus 로고    scopus 로고
    • The protein phosphatase 2C (PP2C) superfamily: Detection of bacterial homologues
    • Bork, P., Brown, N.P., Hegyi, H., and Schultz, J. (1996) The protein phosphatase 2C (PP2C) superfamily: detection of bacterial homologues. Protein Sci 5: 1421-1425.
    • (1996) Protein Sci , vol.5 , pp. 1421-1425
    • Bork, P.1    Brown, N.P.2    Hegyi, H.3    Schultz, J.4
  • 5
    • 0036438894 scopus 로고    scopus 로고
    • Regulation of peptide-chain elongation in mammalian cells
    • Browne, G.J., and Proud, C.G. (2002) Regulation of peptide-chain elongation in mammalian cells. Eur J Biochem 269: 5360-5368.
    • (2002) Eur J Biochem , vol.269 , pp. 5360-5368
    • Browne, G.J.1    Proud, C.G.2
  • 6
    • 0032900603 scopus 로고    scopus 로고
    • Mutational analysis of the role of HPr in Listeria monocytogenes
    • Christensen, D.P., Benson, A.K., and Hutkins, R.W. (1999) Mutational analysis of the role of HPr in Listeria monocytogenes. Appl Environ Microbiol 65: 2112-2115.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2112-2115
    • Christensen, D.P.1    Benson, A.K.2    Hutkins, R.W.3
  • 7
    • 2442645227 scopus 로고    scopus 로고
    • The RNA-binding protein Hfq of Listeria monocytogenes: Role in stress tolerance and virulence
    • Christiansen, J.K., Larsen, M.H., Ingmer, H., Sogaard-Andersen, L., and Kallipolitis, B.H. (2004) The RNA-binding protein Hfq of Listeria monocytogenes: role in stress tolerance and virulence. J Bacteriol 186: 3355-3362.
    • (2004) J Bacteriol , vol.186 , pp. 3355-3362
    • Christiansen, J.K.1    Larsen, M.H.2    Ingmer, H.3    Sogaard-Andersen, L.4    Kallipolitis, B.H.5
  • 8
    • 3042660151 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis protein serine/threonine kinase PknG is linked to cellular glutamate/glutamine levels and is important for growth in vivo
    • Cowley, S., Ko, M., Pick, N., Chow, R., Downing, K.J., Gordhan, B.G., et al. (2004) The Mycobacterium tuberculosis protein serine/threonine kinase PknG is linked to cellular glutamate/glutamine levels and is important for growth in vivo. Mol Microbiol 52: 1691-1702.
    • (2004) Mol Microbiol , vol.52 , pp. 1691-1702
    • Cowley, S.1    Ko, M.2    Pick, N.3    Chow, R.4    Downing, K.J.5    Gordhan, B.G.6
  • 10
    • 0036434714 scopus 로고    scopus 로고
    • Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae
    • Dallo, S.F., Kannan, T.R., Blaylock, M.W., and Baseman, J.B. (2002) Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae. Mol Microbiol 46: 1041-1051.
    • (2002) Mol Microbiol , vol.46 , pp. 1041-1051
    • Dallo, S.F.1    Kannan, T.R.2    Blaylock, M.W.3    Baseman, J.B.4
  • 11
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution
    • Das, A.K., Helps, N.R., Cohen, P.T., and Barford, D. (1996) Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 Å resolution. EMBO J 15: 6798-6809.
    • (1996) EMBO J , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 13
    • 7944222097 scopus 로고    scopus 로고
    • Molecular determinants of Listeria monocytogenes virulence
    • Dussurget, O., Pizarro-Cerda, J., and Cossart, P. (2004) Molecular determinants of Listeria monocytogenes virulence. Annu Rev Microbiol 58: 587-610.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 587-610
    • Dussurget, O.1    Pizarro-Cerda, J.2    Cossart, P.3
  • 14
    • 1842431057 scopus 로고    scopus 로고
    • Protein serine/threonine kinase StkP positively controls virulence and competence in Streptococcus pneumoniae
    • Echenique, J., Kadioglu, A., Romao, S., Andrew, P.W., and Trombe, M.C. (2004) Protein serine/threonine kinase StkP positively controls virulence and competence in Streptococcus pneumoniae. Infect Immun 72: 2434-2437.
    • (2004) Infect Immun , vol.72 , pp. 2434-2437
    • Echenique, J.1    Kadioglu, A.2    Romao, S.3    Andrew, P.W.4    Trombe, M.C.5
  • 15
    • 0036842045 scopus 로고    scopus 로고
    • The PrpC serine-threonine phosphatase and PrkC kinase have opposing physiological roles in stationary-phase Bacillus subtilis cells
    • 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.
    • (2002) J Bacteriol , vol.184 , pp. 6109-6114
    • Gaidenko, T.A.1    Kim, T.J.2    Price, C.W.3
  • 16
    • 0027535009 scopus 로고
    • A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant
    • Galyov, E.E., Hakansson, S., Forsberg, A., and Wolf-Watz, H. (1993) A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant. Nature 361: 730-732.
    • (1993) Nature , vol.361 , pp. 730-732
    • Galyov, E.E.1    Hakansson, S.2    Forsberg, A.3    Wolf-Watz, H.4
  • 17
    • 1842431723 scopus 로고    scopus 로고
    • Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins
    • Granato, D., Bergonzelli, G.E., Pridmore, R.D., Marvin, L., Rouvet, M., and Corthesy-Theulaz, I.E. (2004) Cell surface-associated elongation factor Tu mediates the attachment of Lactobacillus johnsonii NCC533 (La1) to human intestinal cells and mucins. Infect Immun 72: 2160-2169.
    • (2004) Infect Immun , vol.72 , pp. 2160-2169
    • Granato, D.1    Bergonzelli, G.E.2    Pridmore, R.D.3    Marvin, L.4    Rouvet, M.5    Corthesy-Theulaz, I.E.6
  • 18
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S.K., and Hunter, T. (1995) Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J 9: 576-596.
    • (1995) FASEB J , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 19
    • 0024797894 scopus 로고
    • Protein phosphorylation controls translation rates
    • Hershey, J.W. (1989) Protein phosphorylation controls translation rates. J Biol Chem 264: 20823-20826.
    • (1989) J Biol Chem , vol.264 , pp. 20823-20826
    • Hershey, J.W.1
  • 20
    • 0017187684 scopus 로고
    • Abundance and membrane association of elongation factor Tu in E. coli
    • Jacobson, G.R., and Rosenbusch, J.P. (1976) Abundance and membrane association of elongation factor Tu in E. coli. Nature 261: 23-26.
    • (1976) Nature , vol.261 , pp. 23-26
    • Jacobson, G.R.1    Rosenbusch, J.P.2
  • 21
    • 0033404562 scopus 로고    scopus 로고
    • Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: A novel mechanism of protein association at the surface of Gram-positive bacteria
    • Jonquieres, R., Bierne, H., Fiedler, F., Gounon, P., and Cossart, P. (1999) Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of Gram-positive bacteria. Mol Microbiol 34: 902-914.
    • (1999) Mol Microbiol , vol.34 , pp. 902-914
    • Jonquieres, R.1    Bierne, H.2    Fiedler, F.3    Gounon, P.4    Cossart, P.5
  • 22
    • 0027435054 scopus 로고
    • Isolation of the periplasm of Neisseria gonorrhoeae
    • Judd, R.C., and Porcella, S.F. (1993) Isolation of the periplasm of Neisseria gonorrhoeae. Mol Microbiol 10: 567-574.
    • (1993) Mol Microbiol , vol.10 , pp. 567-574
    • Judd, R.C.1    Porcella, S.F.2
  • 23
    • 0036083950 scopus 로고    scopus 로고
    • Identification of Escherichia coli genes that are specifically expressed in a murine model of septicemic infection
    • Khan, M.A., and Isaacson, R.E. (2002) Identification of Escherichia coli genes that are specifically expressed in a murine model of septicemic infection. Infect Immun 70: 3404-3412.
    • (2002) Infect Immun , vol.70 , pp. 3404-3412
    • Khan, M.A.1    Isaacson, R.E.2
  • 24
    • 0027222204 scopus 로고
    • Polarized distribution of Listeria monocytogenes surface protein ActA at the site of directional actin assembly
    • Kocks, C., Hellio, R., Gounon, P., Ohayon, H., and Cossart, P. (1993) Polarized distribution of Listeria monocytogenes surface protein ActA at the site of directional actin assembly. J Cell Sci 105 (Part 3): 699-710.
    • (1993) J Cell Sci , vol.105 , Issue.PART 3 , pp. 699-710
    • Kocks, C.1    Hellio, R.2    Gounon, P.3    Ohayon, H.4    Cossart, P.5
  • 25
    • 0033258542 scopus 로고    scopus 로고
    • Translational regulation by modifications of the elongation factor Tu
    • Kraal, B., Lippmann, C., and Kleanthous, C. (1999) Translational regulation by modifications of the elongation factor Tu. Folia Microbiol (Praha) 44: 131-141.
    • (1999) Folia Microbiol (Praha) , vol.44 , pp. 131-141
    • Kraal, B.1    Lippmann, C.2    Kleanthous, C.3
  • 26
    • 0029811792 scopus 로고    scopus 로고
    • Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells
    • Lebrun, M., Mengaud, J., Ohayon, H., Nato, F., and Cossart, P. (1996) Internalin must be on the bacterial surface to mediate entry of Listeria monocytogenes into epithelial cells. Mol Microbiol 21: 579-592.
    • (1996) Mol Microbiol , vol.21 , pp. 579-592
    • Lebrun, M.1    Mengaud, J.2    Ohayon, H.3    Nato, F.4    Cossart, P.5
  • 27
    • 8744290794 scopus 로고    scopus 로고
    • Identification of the degradome of Isp-1, a major intracellular serine protease of Bacillus subtilis, by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight analysis
    • Lee, A.Y., Goo Park, S., Kho, C.W., Young Park, S., Cho, S., Lee, S.C., et al. (2004) Identification of the degradome of Isp-1, a major intracellular serine protease of Bacillus subtilis, by two-dimensional gel electrophoresis and matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 4: 3437-3445.
    • (2004) Proteomics , vol.4 , pp. 3437-3445
    • Lee, A.Y.1    Goo Park, S.2    Kho, C.W.3    Young Park, S.4    Cho, S.5    Lee, S.C.6
  • 28
    • 0026541096 scopus 로고
    • The expression of virulence genes in Listeria monocytogenes is thermoregulated
    • Leimeister-Wachter, M., Domann, E., and Chakraborty, T. (1992) The expression of virulence genes in Listeria monocytogenes is thermoregulated. J Bacteriol 174: 947-952.
    • (1992) J Bacteriol , vol.174 , pp. 947-952
    • Leimeister-Wachter, M.1    Domann, E.2    Chakraborty, T.3
  • 29
    • 0031722706 scopus 로고    scopus 로고
    • Novel families of putative protein kinases in bacteria and archaea: Evolution of the 'eukaryotic' protein kinase superfamily
    • Leonard, C.J., Aravind, L., and Koonin, E.V. (1998) Novel families of putative protein kinases in bacteria and archaea: evolution of the 'eukaryotic' protein kinase superfamily. Genome Res 8: 1038-1047.
    • (1998) Genome Res , vol.8 , pp. 1038-1047
    • Leonard, C.J.1    Aravind, L.2    Koonin, E.V.3
  • 31
    • 0036428610 scopus 로고    scopus 로고
    • Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes
    • 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.
    • (2002) Mol Microbiol , vol.46 , pp. 571-586
    • Madec, E.1    Laszkiewicz, A.2    Iwanicki, A.3    Obuchowski, M.4    Seror, S.5
  • 32
    • 0035117158 scopus 로고    scopus 로고
    • Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1 beta and inhibits its PKC-mediated nucleotide exchange activity in vitro
    • Mamoun, C.B., and Goldberg, D.E. (2001) Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1 beta and inhibits its PKC-mediated nucleotide exchange activity in vitro. Mol Microbiol 39: 973-981.
    • (2001) Mol Microbiol , vol.39 , pp. 973-981
    • Mamoun, C.B.1    Goldberg, D.E.2
  • 33
    • 0031813669 scopus 로고    scopus 로고
    • Mapping and identification of the major cell wall-associated components of Mycobacterium leprae
    • Marques, M.A., Chitale, S., Brennan, P.J., and Pessolani, M.C. (1998) Mapping and identification of the major cell wall-associated components of Mycobacterium leprae. Infect Immun 66: 2625-2631.
    • (1998) Infect Immun , vol.66 , pp. 2625-2631
    • Marques, M.A.1    Chitale, S.2    Brennan, P.J.3    Pessolani, M.C.4
  • 35
    • 0345146908 scopus 로고    scopus 로고
    • Transcriptome analysis of Listeria monocytogenes identifies three groups of genes differently regulated by PrfA
    • Milohanic, E., Glaser, P., Coppee, J.Y., Frangeul, L., Vega, Y., Vazquez-Boland, J.A., et al. (2003) Transcriptome analysis of Listeria monocytogenes identifies three groups of genes differently regulated by PrfA. Mol Microbiol 47: 1613-1625.
    • (2003) Mol Microbiol , vol.47 , pp. 1613-1625
    • Milohanic, E.1    Glaser, P.2    Coppee, J.Y.3    Frangeul, L.4    Vega, Y.5    Vazquez-Boland, J.A.6
  • 36
    • 0035805492 scopus 로고    scopus 로고
    • A role for the Ppz Ser/Thr protein phosphatases in the regulation of translation elongation factor 1B alpha
    • de Nadal, E., Fadden, R.P., Ruiz, A., Haystead, T., and Arino, J. (2001) A role for the Ppz Ser/Thr protein phosphatases in the regulation of translation elongation factor 1B alpha. J Biol Chem 276: 14829-14834.
    • (2001) J Biol Chem , vol.276 , pp. 14829-14834
    • De Nadal, E.1    Fadden, R.P.2    Ruiz, A.3    Haystead, T.4    Arino, J.5
  • 37
    • 0037146607 scopus 로고    scopus 로고
    • Leishmania EF-1 alpha activates the Src homology 2 domain containing tyrosine phosphatase SHP-1 leading to macrophage deactivation
    • Nandan, D., Yi, T., Lopez, M., Lai, C., and Reiner, N.E. (2002) Leishmania EF-1 alpha activates the Src homology 2 domain containing tyrosine phosphatase SHP-1 leading to macrophage deactivation. J Biol Chem 277: 50190-50197.
    • (2002) J Biol Chem , vol.277 , pp. 50190-50197
    • Nandan, D.1    Yi, T.2    Lopez, M.3    Lai, C.4    Reiner, N.E.5
  • 38
    • 0037487186 scopus 로고    scopus 로고
    • An effective sporulation of Myxococcus xanthus requires glycogen consumption via Pkn4-activated 6-phosphofructokinase
    • Nariya, H., and Inouye, S. (2003) An effective sporulation of Myxococcus xanthus requires glycogen consumption via Pkn4-activated 6-phosphofructokinase. Mol Microbiol 49: 517-528.
    • (2003) Mol Microbiol , vol.49 , pp. 517-528
    • Nariya, H.1    Inouye, S.2
  • 39
    • 0036228110 scopus 로고    scopus 로고
    • StoPK-1, a serine/threonine protein kinase from the glycopeptide antibiotic producer Streptomyces toyocaensis NRRL 15009, affects oxidative stress response
    • Neu, J.M., MacMillan, S.V., Nodwell, J.R., and Wright, G.D. (2002) StoPK-1, a serine/threonine protein kinase from the glycopeptide antibiotic producer Streptomyces toyocaensis NRRL 15009, affects oxidative stress response. Mol Microbiol 44: 417-430.
    • (2002) Mol Microbiol , vol.44 , pp. 417-430
    • Neu, J.M.1    MacMillan, S.V.2    Nodwell, J.R.3    Wright, G.D.4
  • 40
    • 0033801870 scopus 로고    scopus 로고
    • Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family
    • Obuchowski, M., Madec, E., Delattre, D., Boel, G., Iwanicki, A., Foulger, D., and Seror, S.J. (2000) Characterization of PrpC from Bacillus subtilis, a member of the PPM phosphatase family. J Bacteriol 182: 5634-5638.
    • (2000) J Bacteriol , vol.182 , pp. 5634-5638
    • Obuchowski, M.1    Madec, E.2    Delattre, D.3    Boel, G.4    Iwanicki, A.5    Foulger, D.6    Seror, S.J.7
  • 41
    • 0021781999 scopus 로고
    • Mechanism of action of kirromycin-like antibiotics
    • Parmeggiani, A., and Swart, G.W. (1985) Mechanism of action of kirromycin-like antibiotics. Annu Rev Microbiol 39: 557-577.
    • (1985) Annu Rev Microbiol , vol.39 , pp. 557-577
    • Parmeggiani, A.1    Swart, G.W.2
  • 42
    • 0030894214 scopus 로고    scopus 로고
    • A chemically defined minimal medium for the optimal culture of Listeria
    • Phan-Thanh, L., and Gormon, T. (1997) A chemically defined minimal medium for the optimal culture of Listeria. Int J Food Microbiol 35: 91-95.
    • (1997) Int J Food Microbiol , vol.35 , pp. 91-95
    • Phan-Thanh, L.1    Gormon, T.2
  • 43
    • 23044529439 scopus 로고    scopus 로고
    • Measuring and analysing invasion of mammalian cells by bacterial pathogens: The Listeria monocytogenes system
    • Pizarro-Cerdá, J., Lecuit, M., and Cossart, P. (2002) Measuring and analysing invasion of mammalian cells by bacterial pathogens: the Listeria monocytogenes system. Method Microbiol 31: 161-177.
    • (2002) Method Microbiol , vol.31 , pp. 161-177
    • Pizarro-Cerdá, J.1    Lecuit, M.2    Cossart, P.3
  • 45
    • 0037853258 scopus 로고    scopus 로고
    • A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence
    • Rajagopal, L., Clancy, A., and Rubens, C.E. (2003) A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence. J Biol Chem 278: 14429-14441.
    • (2003) J Biol Chem , vol.278 , pp. 14429-14441
    • Rajagopal, L.1    Clancy, A.2    Rubens, C.E.3
  • 46
    • 0032718056 scopus 로고    scopus 로고
    • Signal transduction pathways that regulate eukaryotic protein synthesis
    • Rhoads, R.E. (1999) Signal transduction pathways that regulate eukaryotic protein synthesis. J Biol Chem 274: 30337-30340.
    • (1999) J Biol Chem , vol.274 , pp. 30337-30340
    • Rhoads, R.E.1
  • 47
    • 0028175657 scopus 로고
    • Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli
    • Robertson, E.S., Aggison, L.A., and Nicholson, A.W. (1994) Phosphorylation of elongation factor G and ribosomal protein S6 in bacteriophage T7-infected Escherichia coli. Mol Microbiol 11: 1045-1057.
    • (1994) Mol Microbiol , vol.11 , pp. 1045-1057
    • Robertson, E.S.1    Aggison, L.A.2    Nicholson, A.W.3
  • 49
    • 2442697451 scopus 로고    scopus 로고
    • Regulation of translation elongation and phosphorylation of eEF2 in rat pancreatic acini
    • Sans, M.D., Xie, Q., and Williams, J.A. (2004) Regulation of translation elongation and phosphorylation of eEF2 in rat pancreatic acini. Biochem Biophys Res Commun 319: 144-151.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 144-151
    • Sans, M.D.1    Xie, Q.2    Williams, J.A.3
  • 50
    • 0036838266 scopus 로고    scopus 로고
    • Structural and nucleotide-binding properties of YajQ and YnaF, two Escherichia coli proteins of unknown function
    • Saveanu, C., Miron, S., Borza, T., Craescu, C.T., Labesse, G., Gagyi, C., et al. (2002) Structural and nucleotide-binding properties of YajQ and YnaF, two Escherichia coli proteins of unknown function. Protein Sci 11: 2551-2560.
    • (2002) Protein Sci , vol.11 , pp. 2551-2560
    • Saveanu, C.1    Miron, S.2    Borza, T.3    Craescu, C.T.4    Labesse, G.5    Gagyi, C.6
  • 51
    • 0031764045 scopus 로고    scopus 로고
    • The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: A family portrait
    • Shi, L., Potts, M., and Kennelly, P.J. (1998) The serine, threonine, and/or tyrosine-specific protein kinases and protein phosphatases of prokaryotic organisms: a family portrait. FEMS Microbiol Rev 22: 229-253.
    • (1998) FEMS Microbiol Rev , vol.22 , pp. 229-253
    • Shi, L.1    Potts, M.2    Kennelly, P.J.3
  • 52
    • 0021129964 scopus 로고
    • New shuttle vectors for Bacillus subtilis and Escherichia coli which allow rapid detection of inserted fragments
    • Sullivan, M.A., Yasbin, R.E., and Young, F.E. (1984) New shuttle vectors for Bacillus subtilis and Escherichia coli which allow rapid detection of inserted fragments. Gene 29: 21-26.
    • (1984) Gene , vol.29 , pp. 21-26
    • Sullivan, M.A.1    Yasbin, R.E.2    Young, F.E.3
  • 53
    • 0035044257 scopus 로고    scopus 로고
    • Pph1 from Myxococcus xanthus is a protein phosphatase involved in vegetative growth and development
    • Treuner-Lange, A., Ward, M.J., and Zusman, D.R. (2001) Pph1 from Myxococcus xanthus is a protein phosphatase involved in vegetative growth and development. Mol Microbiol 40: 126-140.
    • (2001) Mol Microbiol , vol.40 , pp. 126-140
    • Treuner-Lange, A.1    Ward, M.J.2    Zusman, D.R.3
  • 54
    • 0036040203 scopus 로고    scopus 로고
    • Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces
    • Umeyama, T., Lee, P.C., and Horinouchi, S. (2002) Protein serine/threonine kinases in signal transduction for secondary metabolism and morphogenesis in Streptomyces. Appl Microbiol Biotechnol 59: 419-425.
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 419-425
    • Umeyama, T.1    Lee, P.C.2    Horinouchi, S.3
  • 56
    • 2942718724 scopus 로고    scopus 로고
    • Protein kinase G from pathogenic mycobacteria promotes survival within macrophages
    • Walburger, A., Koul, A., Ferrari, G., Nguyen, L., Prescianotto-Baschong, C., Huygen, K., et al. (2004) Protein kinase G from pathogenic mycobacteria promotes survival within macrophages. Science 304: 1800-1804.
    • (2004) Science , vol.304 , pp. 1800-1804
    • Walburger, A.1    Koul, A.2    Ferrari, G.3    Nguyen, L.4    Prescianotto-Baschong, C.5    Huygen, K.6
  • 57
    • 0029915601 scopus 로고    scopus 로고
    • Bacterial signalling involving eukaryotic-type protein kinases
    • Zhang, C.C. (1996) Bacterial signalling involving eukaryotic-type protein kinases. Mol Microbiol 20: 9-15.
    • (1996) Mol Microbiol , vol.20 , pp. 9-15
    • Zhang, C.C.1


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