메뉴 건너뛰기




Volumn 350, Issue 5, 2005, Pages 953-963

Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions

Author keywords

Activation loop; Forkhead associated domain; GarA (Rv1827); Ser Thr protein kinase; Substrate docking

Indexed keywords

BACTERIAL PROTEIN; DOCKING PROTEIN; PROTEIN; PROTEIN GARA; PROTEIN PKNB; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 20744445530     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.049     Document Type: Article
Times cited : (131)

References (39)
  • 1
    • 0037005989 scopus 로고    scopus 로고
    • Protein kinases and protein phosphatases in prokaryotes: A genomic perspective
    • P.J. Kennelly Protein kinases and protein phosphatases in prokaryotes: a genomic perspective FEMS Microbiol. Letters 206 2002 1 8
    • (2002) FEMS Microbiol. Letters , vol.206 , pp. 1-8
    • Kennelly, P.J.1
  • 2
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • S.T. Cole, R. Brosch, J. Parkhill, T. Garnier, C. Churcher, and D. Harris Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence Nature 393 1998 537 544
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 3
    • 10744227858 scopus 로고    scopus 로고
    • Disruption of mptpB impairs the ability of Mycobacterium tuberculosis to survive in guinea pigs
    • R. Singh, V. Rao, H. Shakila, R. Gupta, A. Khera, and N. Dhar Disruption of mptpB impairs the ability of Mycobacterium tuberculosis to survive in guinea pigs Mol. Microbiol. 50 2003 751 762
    • (2003) Mol. Microbiol. , vol.50 , pp. 751-762
    • Singh, R.1    Rao, V.2    Shakila, H.3    Gupta, R.4    Khera, A.5    Dhar, N.6
  • 5
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • C.M. Sassetti, D.H. Boyd, and E.J. Rubin Genes required for mycobacterial growth defined by high density mutagenesis Mol. Microbiol. 48 2003 77 84
    • (2003) Mol. Microbiol. , vol.48 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 6
    • 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
    • S. Cowley, M. Ko, N. Pick, R. Chow, K.J. Downing, and B.G. Gordhan 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 2004 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
  • 7
    • 10044253923 scopus 로고
    • Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division
    • J.M. Ghuysen R. Hakenbeck Elsevier Amsterdam
    • M. Matsuhashi Utilization of lipid-linked precursors and the formation of peptidoglycan in the process of cell growth and division J.M. Ghuysen R. Hakenbeck Bacterial Cell Wall 1994 Elsevier Amsterdam 55 71
    • (1994) Bacterial Cell Wall , pp. 55-71
    • Matsuhashi, M.1
  • 9
    • 0141454865 scopus 로고    scopus 로고
    • PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase in Mycobacterium tuberculosis
    • B. Boitel, M. Ortiz-Lombardia, R. Duran, F. Pompeo, S.T. Cole, C. Cerveñansky, and P.M. Alzari PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase in Mycobacterium tuberculosis Mol. Microbiol. 49 2003 1493 1508
    • (2003) Mol. Microbiol. , vol.49 , pp. 1493-1508
    • Boitel, B.1    Ortiz-Lombardia, M.2    Duran, R.3    Pompeo, F.4    Cole, S.T.5    Cerveñansky, C.6    Alzari, P.M.7
  • 11
    • 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
    • L. Rajagopal, A. Clancy, and C.E. Rubens 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 2003 14429 14441
    • (2003) J. Biol. Chem. , vol.278 , pp. 14429-14441
    • Rajagopal, L.1    Clancy, A.2    Rubens, C.E.3
  • 12
    • 14644398001 scopus 로고    scopus 로고
    • Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates
    • L. Nováková, L. Sasková, P. Pallová, J. Janecek, J. Novotná, and A. Ulrych Characterization of a eukaryotic type serine/threonine protein kinase and protein phosphatase of Streptococcus pneumoniae and identification of kinase substrates FEBS J. 272 2005 1243 1254
    • (2005) FEBS J. , vol.272 , pp. 1243-1254
    • Nováková, L.1    Sasková, L.2    Pallová, P.3    Janecek, J.4    Novotná, J.5    Ulrych, A.6
  • 13
    • 0037969625 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis
    • M. Ortiz-Lombardia, F. Pompes, B. Boitel, and P.M. Alzari Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis J. Biol. Chem. 278 2003 13094 13100
    • (2003) J. Biol. Chem. , vol.278 , pp. 13094-13100
    • Ortiz-Lombardia, M.1    Pompes, F.2    Boitel, B.3    Alzari, P.M.4
  • 14
    • 0037337317 scopus 로고    scopus 로고
    • Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases
    • T.A. Young, B. Delagoutte, J.A. Endrizzi, A.M. Falick, and T. Alber Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases Nature Struct. Biol. 10 2003 168 174
    • (2003) Nature Struct. Biol. , vol.10 , pp. 168-174
    • Young, T.A.1    Delagoutte, B.2    Endrizzi, J.A.3    Falick, A.M.4    Alber, T.5
  • 15
    • 0031825604 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins
    • K. Weldingh, I. Rosenkrands, S. Jacobsen, P.B. Rasmussen, M.J. Elhay, and P. Andersen Two-dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins Infect. Immun. 66 1998 3492 3500
    • (1998) Infect. Immun. , vol.66 , pp. 3492-3500
    • Weldingh, K.1    Rosenkrands, I.2    Jacobsen, S.3    Rasmussen, P.B.4    Elhay, M.J.5    Andersen, P.6
  • 17
    • 9044234399 scopus 로고    scopus 로고
    • Mapping of Chlamydia trachomatis proteins by immobiline-polyacrylamide two-dimensional electrophoresis: Spot identification by N-terminal sequencing and immunoblotting
    • L. Bini, M. Sanchez-Campillo, A. Santucci, B. Magi, B. Marzocchi, and M. Comanducci Mapping of Chlamydia trachomatis proteins by immobiline- polyacrylamide two-dimensional electrophoresis: spot identification by N-terminal sequencing and immunoblotting Electrophoresis 17 1996 185 190
    • (1996) Electrophoresis , vol.17 , pp. 185-190
    • Bini, L.1    Sanchez-Campillo, M.2    Santucci, A.3    Magi, B.4    Marzocchi, B.5    Comanducci, M.6
  • 18
    • 0030862226 scopus 로고    scopus 로고
    • Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry
    • M.G. Sonnenberg, and J.T. Belisle Definition of Mycobacterium tuberculosis culture filtrate proteins by two-dimensional polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and electrospray mass spectrometry Infect. Immun. 65 1997 4515 4524
    • (1997) Infect. Immun. , vol.65 , pp. 4515-4524
    • Sonnenberg, M.G.1    Belisle, J.T.2
  • 19
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • M. Mann, and O.N. Jensen Proteomic analysis of post-translational modifications Nature Biotechnol. 21 2004 255 261
    • (2004) Nature Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 20
    • 0031825604 scopus 로고    scopus 로고
    • Two dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins
    • K. Weldingh, I. Rosenkrands, S. Jacobsen, P.B. Rasmussen, M.J. Elhay, and P. Andersen Two dimensional electrophoresis for analysis of Mycobacterium tuberculosis culture filtrate and purification and characterization of six novel proteins Infect. Immun. 66 1998 3492 3500
    • (1998) Infect. Immun. , vol.66 , pp. 3492-3500
    • Weldingh, K.1    Rosenkrands, I.2    Jacobsen, S.3    Rasmussen, P.B.4    Elhay, M.J.5    Andersen, P.6
  • 21
    • 0033007066 scopus 로고    scopus 로고
    • Immunological evaluation of novel Mycobacterium tuberculosis culture filtrate proteins
    • K. Weldingh, and P. Andersen Immunological evaluation of novel Mycobacterium tuberculosis culture filtrate proteins FEMS Immunol. Med. Microbiol. 23 1999 159 164
    • (1999) FEMS Immunol. Med. Microbiol. , vol.23 , pp. 159-164
    • Weldingh, K.1    Andersen, P.2
  • 23
    • 0032724559 scopus 로고    scopus 로고
    • Exponential-phase glycogen recycling is essential for growth of Mycobacterium smegmatis
    • A.E. Belanger, and G.F. Hatfull Exponential-phase glycogen recycling is essential for growth of Mycobacterium smegmatis J. Bacteriol. 181 1999 6670 6678
    • (1999) J. Bacteriol. , vol.181 , pp. 6670-6678
    • Belanger, A.E.1    Hatfull, G.F.2
  • 24
    • 0031795119 scopus 로고    scopus 로고
    • Protein tyrosine kinases: Structure, substrate specificity, and drug discovery
    • F.A. al-Obeidi, J.J. Wu, and K.S. Lam Protein tyrosine kinases: structure, substrate specificity, and drug discovery Biopolymers 47 1998 197 223
    • (1998) Biopolymers , vol.47 , pp. 197-223
    • Al-Obeidi, F.A.1    Wu, J.J.2    Lam, K.S.3
  • 25
    • 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
    • E. Madec, A. Stensballe, S. Kjellstrom, L. Cladiere, M. Obuchowski, O.N. Jensen, and S.J. Seror 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. 330 2003 459 472
    • (2003) J. Mol. Biol. , vol.330 , pp. 459-472
    • Madec, E.1    Stensballe, A.2    Kjellstrom, S.3    Cladiere, L.4    Obuchowski, M.5    Jensen, O.N.6    Seror, S.J.7
  • 26
    • 0348223992 scopus 로고    scopus 로고
    • An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis
    • V. Molle, L. Kremer, C. Girard-Blanc, G.S. Besra, A.J. Cozzone, and J.F. Prost An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis Biochemistry 42 2003 15300 15309
    • (2003) Biochemistry , vol.42 , pp. 15300-15309
    • Molle, V.1    Kremer, L.2    Girard-Blanc, C.3    Besra, G.S.4    Cozzone, A.J.5    Prost, J.F.6
  • 27
    • 2342467904 scopus 로고    scopus 로고
    • Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis
    • V. Molle, D. Soulat, J.M. Jault, C. Grangeasse, A.J. Cozzone, and J.F. Prost Two FHA domains on an ABC transporter, Rv1747, mediate its phosphorylation by PknF, a Ser/Thr protein kinase from Mycobacterium tuberculosis FEMS Microbiol. Letters 234 2004 215 223
    • (2004) FEMS Microbiol. Letters , vol.234 , pp. 215-223
    • Molle, V.1    Soulat, D.2    Jault, J.M.3    Grangeasse, C.4    Cozzone, A.J.5    Prost, J.F.6
  • 29
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • R.M. Biondi, and A.R. Nebreda Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions Biochem. J. 372 2003 1 13
    • (2003) Biochem. J. , vol.372 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 30
    • 0042470439 scopus 로고    scopus 로고
    • Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling
    • S.J. Lee, M.F. Schwartz, J.K. Duong, and D.F. Stern Rad53 phosphorylation site clusters are important for Rad53 regulation and signaling Mol. Cell. Biol. 23 2003 6300 6314
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 6300-6314
    • Lee, S.J.1    Schwartz, M.F.2    Duong, J.K.3    Stern, D.F.4
  • 31
    • 0346156078 scopus 로고    scopus 로고
    • Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor
    • J. Hu, J. Liu, R. Ghirlando, A.R. Saltiel, and S.R. Hubbard Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor Mol. Cell. 12 2003 1379 1389
    • (2003) Mol. Cell. , vol.12 , pp. 1379-1389
    • Hu, J.1    Liu, J.2    Ghirlando, R.3    Saltiel, A.R.4    Hubbard, S.R.5
  • 32
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA domain: Phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
    • D. Durocher, I.A. Taylor, D. Sarbassova, L.F. Haire, S.L. Westcott, and S.P. Jackson The molecular basis of FHA domain: phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms Mol. Cell. 6 2000 1169 1182
    • (2000) Mol. Cell. , vol.6 , pp. 1169-1182
    • Durocher, D.1    Taylor, I.A.2    Sarbassova, D.3    Haire, L.F.4    Westcott, S.L.5    Jackson, S.P.6
  • 33
    • 0344255640 scopus 로고    scopus 로고
    • Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions
    • H. Li, I.J. Byeon, Y. Ju, and M.D. Tsai Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions J. Mol. Biol. 335 2004 371 381
    • (2004) J. Mol. Biol. , vol.335 , pp. 371-381
    • Li, H.1    Byeon, I.J.2    Ju, Y.3    Tsai, M.D.4
  • 34
    • 2342573665 scopus 로고    scopus 로고
    • Identifying protein kinase substrates: Hunting for the organ-grinder's monkeys
    • D.C. Berwick, and J.M. Tavaré Identifying protein kinase substrates: hunting for the organ-grinder's monkeys Trends Biochem. Sci. 29 2004 227 232
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 227-232
    • Berwick, D.C.1    Tavaré, J.M.2
  • 35
    • 0027980597 scopus 로고
    • Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase
    • A. Matsumoto, S.K. Hong, H. Ishizuka, S. Horinouchi, and T. Beppu Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase Gene 146 1994 47 56
    • (1994) Gene , vol.146 , pp. 47-56
    • Matsumoto, A.1    Hong, S.K.2    Ishizuka, H.3    Horinouchi, S.4    Beppu, T.5
  • 36
    • 0036886406 scopus 로고    scopus 로고
    • Activation of 6-phosphofructokinase via phosphorylation by Pkn4, a protein Ser/Thr kinase of Myxococcus xanthus
    • H. Nariya, and S. Inouye Activation of 6-phosphofructokinase via phosphorylation by Pkn4, a protein Ser/Thr kinase of Myxococcus xanthus Mol. Microbiol. 46 2002 1353 1366
    • (2002) Mol. Microbiol. , vol.46 , pp. 1353-1366
    • Nariya, H.1    Inouye, S.2
  • 37
    • 0032847036 scopus 로고    scopus 로고
    • Comparative proteome analysis of Mycobacterium tuberculosis and M. bovis BCG strains: Towards functional genomics of microbial pathogens
    • P.R. Jungblut, U.E. Schaible, H.J. Mollenkopf, U. Zimny-Arndt, B. Raupach, and J. Mattow Comparative proteome analysis of Mycobacterium tuberculosis and M. bovis BCG strains: towards functional genomics of microbial pathogens Mol. Microbiol. 33 1999 1103 1117
    • (1999) Mol. Microbiol. , vol.33 , pp. 1103-1117
    • Jungblut, P.R.1    Schaible, U.E.2    Mollenkopf, H.J.3    Zimny-Arndt, U.4    Raupach, B.5    Mattow, J.6
  • 38
    • 0034009520 scopus 로고    scopus 로고
    • Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • P. Schuck Size distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.