메뉴 건너뛰기




Volumn 257, Issue 1, 1998, Pages 55-61

Characterisation of two putative protein Ser/Thr kinases from actinomycete Streptomyces granaticolor both endowed with different properties

Author keywords

Autophosphorylation; Protein Ser Thr kinase; Signal transduction; Streptomyces granaticolor

Indexed keywords

PROTEIN SERINE THREONINE KINASE;

EID: 0032189505     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2570055.x     Document Type: Article
Times cited : (24)

References (35)
  • 1
    • 0024398149 scopus 로고
    • Protein phosphorylation and regulation of adaptive responses in bacteria
    • Stock, J. B., Ninfa, A. J. & Stock, A. M. (1989) Protein phosphorylation and regulation of adaptive responses in bacteria, Microbiol. Rev. 53, 450-490.
    • (1989) Microbiol. Rev. , vol.53 , pp. 450-490
    • Stock, J.B.1    Ninfa, A.J.2    Stock, A.M.3
  • 2
    • 0025790172 scopus 로고
    • A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium
    • Munoz-Dorado, J., Inouye, S. & Inouye, M. (1991) A gene encoding a protein serine/threonine kinase is required for normal development of M. xanthus, a gram-negative bacterium, Cell 67, 995-1006.
    • (1991) Cell , vol.67 , pp. 995-1006
    • Munoz-Dorado, J.1    Inouye, S.2    Inouye, M.3
  • 3
    • 0028986249 scopus 로고
    • Myxococcus xanthus, a gram-negative bacterium, contains a transmembrane protein serine/threonine kinase that blocks the secretion of beta-lactamase by phosphorylation
    • Udo, H., Munoz-Dorado, J., Inouye, M. & Inouye, S. (1995) Myxococcus xanthus, a gram-negative bacterium, contains a transmembrane protein serine/threonine kinase that blocks the secretion of beta-lactamase by phosphorylation, Genes Dev. 9, 972-983.
    • (1995) Genes Dev. , vol.9 , pp. 972-983
    • Udo, H.1    Munoz-Dorado, J.2    Inouye, M.3    Inouye, S.4
  • 4
    • 0029971544 scopus 로고    scopus 로고
    • Reciprocal regulation of the differentiation of Myxococcus xanthus by Pkn5 and Pkn6, eukaryotic-like Ser/Thr protein kinases
    • Zhang, W., Inouye, M. & Inouye, S. (1996) Reciprocal regulation of the differentiation of Myxococcus xanthus by Pkn5 and Pkn6, eukaryotic-like Ser/Thr protein kinases, Mol. Microbiol. 20, 435-447.
    • (1996) Mol. Microbiol. , vol.20 , pp. 435-447
    • Zhang, W.1    Inouye, M.2    Inouye, S.3
  • 5
    • 0031016266 scopus 로고    scopus 로고
    • Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus
    • Hanlon, W. A., Inouye, M. & Inouye, S. (1997) Pkn9, a Ser/Thr protein kinase involved in the development of Myxococcus xanthus, Mol. Microbiol. 23, 459-471.
    • (1997) Mol. Microbiol. , vol.23 , pp. 459-471
    • Hanlon, W.A.1    Inouye, M.2    Inouye, S.3
  • 6
    • 0027146285 scopus 로고
    • A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120
    • Zhang, C. C. (1993) A gene encoding a protein related to eukaryotic protein kinases from the filamentous heterocystous cyanobacterium Anabaena PCC 7120, Proc. Natl Acad. Sci. USA 90, 11840-11844.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11840-11844
    • Zhang, C.C.1
  • 7
    • 0027980597 scopus 로고
    • Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase
    • Matsumoto, A., Hong, S. K., Ishizuka, H., Horinouchi, S. & Beppu, T. (1994) Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase, Gene (Amst.) 146, 47-56.
    • (1994) Gene (Amst.) , vol.146 , pp. 47-56
    • Matsumoto, A.1    Hong, S.K.2    Ishizuka, H.3    Horinouchi, S.4    Beppu, T.5
  • 8
    • 0028850850 scopus 로고
    • Cloning, sequencing and expression of serine/threonine kinase-encoding genes from Streptomyces coelicolor A3(2)
    • Urabe, H. & Ogawara, H. (1995) Cloning, sequencing and expression of serine/threonine kinase-encoding genes from Streptomyces coelicolor A3(2), Gene (Amst.) 153, 99-104.
    • (1995) Gene (Amst.) , vol.153 , pp. 99-104
    • Urabe, H.1    Ogawara, H.2
  • 9
    • 0030002810 scopus 로고    scopus 로고
    • A deduced Thermomonospora curvata protein containing serine/threonine protein kinase and WD-repeat domains
    • Janda, L., Tichý, P., Spížek, J. & Petříček, M. (1996) A deduced Thermomonospora curvata protein containing serine/threonine protein kinase and WD-repeat domains, J. Bacteriol. 178, 1487-1489.
    • (1996) J. Bacteriol. , vol.178 , pp. 1487-1489
    • Janda, L.1    Tichý, P.2    Spížek, J.3    Petříček, M.4
  • 10
    • 0031039634 scopus 로고    scopus 로고
    • A serine/threonine protein kinase from Mycobacterium tuberculosis
    • Peirs, P., De Wit, L., Braibant, M., Huygen, K. & Content, J. (1997) A serine/threonine protein kinase from Mycobacterium tuberculosis, Eur. J. Biochem. 244, 604-612.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 604-612
    • Peirs, P.1    De Wit, L.2    Braibant, M.3    Huygen, K.4    Content, J.5
  • 13
    • 0027384770 scopus 로고
    • Genetics of differentiation in Streptomyces
    • Chater, K. F. (1993) Genetics of differentiation in Streptomyces, Annu. Rev. Microbiol. 47, 685-713.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 685-713
    • Chater, K.F.1
  • 14
    • 0028840854 scopus 로고
    • Protein phosphorylation in submerged spores and vegetative mycelium of Streptomyces granaticolor
    • Janeček, J., Moravec, V., Dobrová, Z., Janda, I. & Weiser, J. (1995) Protein phosphorylation in submerged spores and vegetative mycelium of Streptomyces granaticolor, FEMS Microbiol. Lett. 133, 91-94.
    • (1995) FEMS Microbiol. Lett. , vol.133 , pp. 91-94
    • Janeček, J.1    Moravec, V.2    Dobrová, Z.3    Janda, I.4    Weiser, J.5
  • 15
    • 0014225070 scopus 로고
    • Taxonomic characteristic of the strain ETH 7437 producing granaticin
    • Řičicová, A. & Řeháček, Z. (1968) Taxonomic characteristic of the strain ETH 7437 producing granaticin, Folia Microbiol. 13, 346-349.
    • (1968) Folia Microbiol. , vol.13 , pp. 346-349
    • Řičicová, A.1    Řeháček, Z.2
  • 16
    • 0000632797 scopus 로고
    • TnphoA: A transposon probe for protein export signals
    • Manoil, C. & Beckwith, J. (1985) TnphoA: a transposon probe for protein export signals, Proc. Natl Acad. Sci. USA 82, 8129-8133.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 8129-8133
    • Manoil, C.1    Beckwith, J.2
  • 19
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • Hanks, S. K., Quinn, A. M. & Hunter, T. (1988) The protein kinase family: conserved features and deduced phylogeny of the catalytic domains, Science 241, 42-52.
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 20
    • 0028070249 scopus 로고
    • Nucleotide imbalance and polymerase chain reaction: Effects on DNA amplification and synthesis of high specific activity radiolabeled DNA probes
    • Mertz, L. M. & Rashtchian, A. (1994) Nucleotide imbalance and polymerase chain reaction: effects on DNA amplification and synthesis of high specific activity radiolabeled DNA probes, Anal. Biochem. 221, 160-165.
    • (1994) Anal. Biochem. , vol.221 , pp. 160-165
    • Mertz, L.M.1    Rashtchian, A.2
  • 21
    • 0021710537 scopus 로고
    • The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences
    • Bibb, M. J., Findlay, P. R. & Johnson, M. W. (1984) The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences, Gene (Amst.) 30, 157-166.
    • (1984) Gene (Amst.) , vol.30 , pp. 157-166
    • Bibb, M.J.1    Findlay, P.R.2    Johnson, M.W.3
  • 22
    • 0000207681 scopus 로고
    • TMbase - A database of membrane spanning protein segments
    • Hofmann, K. & Stoffel, W. (1993) TMbase - A database of membrane spanning protein segments, Biol. Chem. Hoppe Seyler 347, 166.
    • (1993) Biol. Chem. Hoppe Seyler , vol.347 , pp. 166
    • Hofmann, K.1    Stoffel, W.2
  • 23
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D. & Zakour, R. A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection, Methods Enzymol. 154, 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 24
    • 7344263588 scopus 로고    scopus 로고
    • One-tube, two stage PCR-directed in vitro mutagenesis using megaprimers
    • T01122
    • Ekici, A. B., Park, O. S., Fuchs, C. & Rautenstrauss, B. (1997) One-tube, two stage PCR-directed in vitro mutagenesis using megaprimers, Technical Tips Online (http://www.elsevier.com/locate/tto) T01122.
    • (1997) Technical Tips Online
    • Ekici, A.B.1    Park, O.S.2    Fuchs, C.3    Rautenstrauss, B.4
  • 25
    • 0020393472 scopus 로고
    • Endogenous protein phosphorylation in Escherichia coli extracts
    • Manai, M. & Cozzone, A. J. (1982) Endogenous protein phosphorylation in Escherichia coli extracts, Biochem. Biophys. Res. Commun. 107, 981-988.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 981-988
    • Manai, M.1    Cozzone, A.J.2
  • 26
    • 0024558784 scopus 로고
    • Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins
    • Kamps, M. P. & Sefton, B. M. (1989) Acid and base hydrolysis of phosphoproteins bound to immobilon facilitates analysis of phosphoamino acids in gel-fractionated proteins, Anal. Biochem. 176, 22-27.
    • (1989) Anal. Biochem. , vol.176 , pp. 22-27
    • Kamps, M.P.1    Sefton, B.M.2
  • 27
    • 0011864425 scopus 로고
    • Fusions of secreted proteins to alkaline phosphatase: An approach for studying protein secretion
    • Hoffman, C. S. & Wright, A. (1985) Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion, Proc. Natl Acad. Sci. USA 82, 5107-5111.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 5107-5111
    • Hoffman, C.S.1    Wright, A.2
  • 28
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and 80 transducing phages
    • Brickman, E. & Beckwith, J. (1975) Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and 80 transducing phages, J. Mol. Biol. 96, 307-316.
    • (1975) J. Mol. Biol. , vol.96 , pp. 307-316
    • Brickman, E.1    Beckwith, J.2
  • 29
    • 0029643953 scopus 로고
    • The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A
    • Ghosh, M., Anthony, C., Harlos, K., Goodwin, M. G. & Blake, C. (1995) The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A, Structure 3, 177-187.
    • (1995) Structure , vol.3 , pp. 177-187
    • Ghosh, M.1    Anthony, C.2    Harlos, K.3    Goodwin, M.G.4    Blake, C.5
  • 30
    • 0029043812 scopus 로고
    • The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens
    • Cozier, G. E., Giles, I. G. & Anthony, C. (1995) The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens, Biochem. J. 308, 375-379.
    • (1995) Biochem. J. , vol.308 , pp. 375-379
    • Cozier, G.E.1    Giles, I.G.2    Anthony, C.3
  • 32
    • 0027535009 scopus 로고
    • A secreted protein kinase of Yersinia pseudotuberculosis is an indispensable virulence determinant
    • Galyov, E. E., Hakansson, S., Forsberg, A. & 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
  • 33
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • Hartmann, E., Rapoport, T. A. & Lodish, H. F. (1989) Predicting the orientation of eukaryotic membrane-spanning proteins, Proc. Natl Acad. Sci. USA 86, 5786-5790.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 34
    • 0030907121 scopus 로고    scopus 로고
    • Two genes encoding an endoglucanase and a cellulose-binding protein are clustered and co-regulated by a TTA codon in Streptomyces halstedii JM8
    • Garda, A. L., Fernandez Abalos, J. M., Sanchez, P., Ruiz Arribas, A. & Santamaria, R. I. (1997) Two genes encoding an endoglucanase and a cellulose-binding protein are clustered and co-regulated by a TTA codon in Streptomyces halstedii JM8. Biochem. J. 324, 403-411.
    • (1997) Biochem. J. , vol.324 , pp. 403-411
    • Garda, A.L.1    Fernandez Abalos, J.M.2    Sanchez, P.3    Ruiz Arribas, A.4    Santamaria, R.I.5
  • 35
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L. N., Noble, M. E. & Owen, D. J. (1996) Active and inactive protein kinases: structural basis for regulation, Cell 85, 149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.