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Volumn 38, Issue 6, 2005, Pages 695-702

Cloning and molecular characterization of groESL heat-shock operon in methylotrophic bacterium Methylovorus sp. strain SS1 DSM 11726

Author keywords

GroESL; Heat shock operon; Methylosinus sp. SS1; Methylotrophic bacteria

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; METHYLOSINUS; METHYLOSINUS SP.; METHYLOVORUS;

EID: 32644452284     PISSN: 12258687     EISSN: 12258687     Source Type: Journal    
DOI: 10.5483/bmbrep.2005.38.6.695     Document Type: Review
Times cited : (4)

References (48)
  • 1
    • 0026343040 scopus 로고
    • Biological role and regulation of the universally conserved heat shock proteins
    • Ang, D., Liberek, K., Skowyra, D., Zylicz, M. and Georgopoulos, C. (1991) Biological role and regulation of the universally conserved heat shock proteins. J. Biol. Chem. 266, 24233-24236.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24233-24236
    • Ang, D.1    Liberek, K.2    Skowyra, D.3    Zylicz, M.4    Georgopoulos, C.5
  • 2
    • 0030027663 scopus 로고    scopus 로고
    • Expression of the groESL operon is cell-cycle controlled in Caulobacter crescentus
    • Avedissian, M., and Lopes Gomes, S. (1996) Expression of the groESL operon is cell-cycle controlled in Caulobacter crescentus. Mol. Microbiol. 19, 79-89.
    • (1996) Mol. Microbiol. , vol.19 , pp. 79-89
    • Avedissian, M.1    Lopes Gomes, S.2
  • 3
    • 0030047969 scopus 로고    scopus 로고
    • Two different mechanisms are involved in the heat-shock regulation of chaperonin gene expression in Bradyrhizobium japonicum
    • Babst, M., Hennecke, H. and Fischer, H. M. (1996) Two different mechanisms are involved in the heat-shock regulation of chaperonin gene expression in Bradyrhizobium japonicum. Mol. Microbiol. 19, 827-839.
    • (1996) Mol. Microbiol. , vol.19 , pp. 827-839
    • Babst, M.1    Hennecke, H.2    Fischer, H.M.3
  • 4
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker, J. and Craig, E. A. (1994) Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219, 11-23.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11-23
    • Becker, J.1    Craig, E.A.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem, 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0026630452 scopus 로고
    • Use of 16S rRNA analysis to investigate phylogeny of methylotrophic bacteria
    • Bratina, B. J., Brusseau, G A. and Hanson, R. S. (1992) Use of 16S rRNA analysis to investigate phylogeny of methylotrophic bacteria Intl. J. Syst. Bacteriol. 42, 645-648.
    • (1992) Intl. J. Syst. Bacteriol. , vol.42 , pp. 645-648
    • Bratina, B.J.1    Brusseau, G.A.2    Hanson, R.S.3
  • 10
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E. A., Gambill, B. D. and Nelson, R. J. (1993) Heat shock proteins: molecular chaperones of protein biogenesis. Micmbiol. Rev. 57, 402-414.
    • (1993) Micmbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 12
    • 0037206535 scopus 로고    scopus 로고
    • Cloning, molecular characterization, and transcriptional analysis of dnaK. operon in a methylotrophic bacterium Methylovorus sp. strain SS1 DSM 11726
    • Eom, C. Y., Park, S. T., Kim, E., Ro, Y. T., Kim, S. W. and Kim, Y. M. (2002) Cloning, molecular characterization, and transcriptional analysis of dnaK. operon in a methylotrophic bacterium Methylovorus sp. strain SS1 DSM 11726. Mol. Cells 14, 245-254.
    • (2002) Mol. Cells , vol.14 , pp. 245-254
    • Eom, C.Y.1    Park, S.T.2    Kim, E.3    Ro, Y.T.4    Kim, S.W.5    Kim, Y.M.6
  • 13
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt, K. L., Hendrick, J. P., Houry, W. A. and Haiti, F. U. (1997) In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90, 491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Haiti, F.U.4
  • 14
    • 0024554107 scopus 로고
    • The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
    • Fayet, O., Ziegelhoffer, T. and Georgopoulos, C. (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171, 1379-1385.
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 15
    • 0029924864 scopus 로고    scopus 로고
    • Cloning, characterization and functional analysis of groEL-like gene from thermophilic cyanobacterium Synechococcus vulcanus, which does not form an operon with groES
    • Furuki, M., Tanaka, N., Hiyama, T. and Nakamoto, H. (1996) Cloning, characterization and functional analysis of groEL-like gene from thermophilic cyanobacterium Synechococcus vulcanus, which does not form an operon with groES. Biochim. Biophys. Acta 1294, 106-110.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 106-110
    • Furuki, M.1    Tanaka, N.2    Hiyama, T.3    Nakamoto, H.4
  • 16
    • 0027333423 scopus 로고
    • Role of the major heat shock proteins as molecular chaperones
    • Georgopoulos, C. and Welch, W. J. (1993) Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol. 9, 601-634.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 601-634
    • Georgopoulos, C.1    Welch, W.J.2
  • 17
    • 0021223667 scopus 로고
    • Cloning and expression in Pseudomonas aeruginosa of a gene involved in the production of alginate
    • Goldberg, J. B. and Ohman, D. E. (1984) Cloning and expression in Pseudomonas aeruginosa of a gene involved in the production of alginate. J. Bacteriol. 158, 1115-1121.
    • (1984) J. Bacteriol. , vol.158 , pp. 1115-1121
    • Goldberg, J.B.1    Ohman, D.E.2
  • 18
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 19
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F. U. and Hayer-Hartl, M. (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 20
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker, M., Schumann, W. and Volker, U. (1996) Heat-shock and general stress response in Bacillus subtilis. Mol. Microbiol. 19, 417-428.
    • (1996) Mol. Microbiol. , vol.19 , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Volker, U.3
  • 21
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick, J. P. and Hartl, F. U. (1993) Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 22
    • 0027214204 scopus 로고
    • Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
    • Horwich, A. L., Low, K. B., Fenton, W. A., Hirshfield, I. N. and Furtak, K. (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74, 909-917.
    • (1993) Cell , vol.74 , pp. 909-917
    • Horwich, A.L.1    Low, K.B.2    Fenton, W.A.3    Hirshfield, I.N.4    Furtak, K.5
  • 23
    • 0034856940 scopus 로고    scopus 로고
    • Chaperone-assisted protein folding in the cell cytoplasm
    • Houry, W. A. (2001) Chaperone-assisted protein folding in the cell cytoplasm. Curr. Protein Pept. Sci. 2, 227-244.
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 227-244
    • Houry, W.A.1
  • 24
    • 0030895817 scopus 로고    scopus 로고
    • Cloning, nucleotide sequence, and regulatory analysis of the Nitrosomonas europaea dnaK gene
    • lizumi, T. and Nakamura, K. (1997) Cloning, nucleotide sequence, and regulatory analysis of the Nitrosomonas europaea dnaK gene. Appl. Environ. Microbiol. 63, 1777-1784.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1777-1784
    • Lizumi, T.1    Nakamura, K.2
  • 25
    • 0019855290 scopus 로고
    • Purification and some properties of carbon monoxide dehydrogenase from Pseudomonas carboxydohydrogena
    • Kim, Y. M. and Hegeman, G. D. (1981) Purification and some properties of carbon monoxide dehydrogenase from Pseudomonas carboxydohydrogena. J. Bacteriol. 148, 904-911.
    • (1981) J. Bacteriol. , vol.148 , pp. 904-911
    • Kim, Y.M.1    Hegeman, G.D.2
  • 26
    • 0031014025 scopus 로고    scopus 로고
    • Cloning and characterization of two groESL operons of Rhodobacter sphaeroides: Transcriptional regulation of the heat-induced groESL operon
    • Lee, W. T. Terlesky, K. C. and Tabita, F. R. (1997) Cloning and characterization of two groESL operons of Rhodobacter sphaeroides: transcriptional regulation of the heat-induced groESL operon. J. Bacteriol. 179, 487-495.
    • (1997) J. Bacteriol. , vol.179 , pp. 487-495
    • Lee, W.T.1    Terlesky, K.C.2    Tabita, F.R.3
  • 27
    • 0025168744 scopus 로고
    • Methylotrophs: Genetics and commercial applications
    • Lidstrom, M. E. and Stirling, D. I. (1990) Methylotrophs: genetics and commercial applications. Annu. Rev. Micmbiol. 44, 27-58.
    • (1990) Annu. Rev. Micmbiol. , vol.44 , pp. 27-58
    • Lidstrom, M.E.1    Stirling, D.I.2
  • 29
    • 0027525938 scopus 로고
    • The strongly conserved carboxylterminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable
    • McLennan, N. F., Girshovich, A. S., Lissin, N. M., Charters, Y. and Masters, M. (1993) The strongly conserved carboxylterminus glycine-methionine motif of the Escherichia coli GroEL chaperonin is dispensable. Mol. Microbiol. 7, 49-58.
    • (1993) Mol. Microbiol. , vol.7 , pp. 49-58
    • McLennan, N.F.1    Girshovich, A.S.2    Lissin, N.M.3    Charters, Y.4    Masters, M.5
  • 30
    • 0030849142 scopus 로고    scopus 로고
    • The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis
    • Mogk, A., Homuth, G., Scholz, C., Kim, L., Schmid, F. X. and Schumann, W. (1997) The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J. 16, 4579-4590.
    • (1997) EMBO J. , vol.16 , pp. 4579-4590
    • Mogk, A.1    Homuth, G.2    Scholz, C.3    Kim, L.4    Schmid, F.X.5    Schumann, W.6
  • 31
    • 0346657488 scopus 로고    scopus 로고
    • Stress-shock response of a methylotrophic bacterium Methylovorus sp. strain SS1 DSM 11726
    • Park, J. H., Kim, S. W., Kim, E., Ro, Y. T. and Kim, Y. M. (2001) Stress-shock response of a methylotrophic bacterium Methylovorus sp. strain SS1 DSM 11726. J. Microbiol. 37, 162-167.
    • (2001) J. Microbiol. , vol.37 , pp. 162-167
    • Park, J.H.1    Kim, S.W.2    Kim, E.3    Ro, Y.T.4    Kim, Y.M.5
  • 32
    • 0035962902 scopus 로고    scopus 로고
    • Cloning and characterization of the major groESL operon from a nitrogen-fixing cyanobacterium Anabaena sp. strain L-31
    • Rajaram, H., Ballal, A. D., Apte, S. K., Wiegert, T. and Schumann, W. (2001) Cloning and characterization of the major groESL operon from a nitrogen-fixing cyanobacterium Anabaena sp. strain L-31. Biochim. Biophys. Acta 1519, 143-146.
    • (2001) Biochim. Biophys. Acta , vol.1519 , pp. 143-146
    • Rajaram, H.1    Ballal, A.D.2    Apte, S.K.3    Wiegert, T.4    Schumann, W.5
  • 33
    • 0029944771 scopus 로고    scopus 로고
    • Identification of a Caulobacter crescentus operon encoding hrcA, involved in negatively regulating heat-inducible transcription, and the chaperone gene grpE
    • Roberts, R. C., Toochinda, C., Avedissian, M., Baldini, R. L., Gomes, S. L. and Shapiro, L. (1996) Identification of a Caulobacter crescentus operon encoding hrcA, involved in negatively regulating heat-inducible transcription, and the chaperone gene grpE. J. Bacterial. 178, 1829-1841.
    • (1996) J. Bacterial. , vol.178 , pp. 1829-1841
    • Roberts, R.C.1    Toochinda, C.2    Avedissian, M.3    Baldini, R.L.4    Gomes, S.L.5    Shapiro, L.6
  • 34
    • 0027483509 scopus 로고
    • Cloning and characterization of multiple groEL chaperonin-encoding genes in Rhizobium meliloti
    • Rusanganwa, E. and Gupta, R. S. (1993) Cloning and characterization of multiple groEL chaperonin-encoding genes in Rhizobium meliloti. Gene 126, 67-75.
    • (1993) Gene , vol.126 , pp. 67-75
    • Rusanganwa, E.1    Gupta, R.S.2
  • 37
    • 0027276270 scopus 로고
    • Heat shock transcription of the groESL operon of Agrobacterium tumefaciens may involve a hairpin-loop structure
    • Segal, G. and Ron, E. Z. (1993) Heat shock transcription of the groESL operon of Agrobacterium tumefaciens may involve a hairpin-loop structure. J. Bacteriol. 175, 3083-3088.
    • (1993) J. Bacteriol. , vol.175 , pp. 3083-3088
    • Segal, G.1    Ron, E.Z.2
  • 38
    • 0029890428 scopus 로고    scopus 로고
    • Heat shock activation of the groESL operon of Agrobacterium tumefaciens and the regulatory roles of the inverted repeat
    • Segal, G. and Ron, E. Z. (1996) Heat shock activation of the groESL operon of Agrobacterium tumefaciens and the regulatory roles of the inverted repeat. J. Bacteriol. 178, 3634-3640.
    • (1996) J. Bacteriol. , vol.178 , pp. 3634-3640
    • Segal, G.1    Ron, E.Z.2
  • 39
    • 0031873712 scopus 로고    scopus 로고
    • Regulation of heat-shock response in bacteria
    • Segal, G. and Ron, E. Z. (1998) Regulation of heat-shock response in bacteria. Ann. New York Acad Sci. 851, 147-151.
    • (1998) Ann. New York Acad Sci. , vol.851 , pp. 147-151
    • Segal, G.1    Ron, E.Z.2
  • 40
    • 0347532865 scopus 로고
    • Isolation and characterization of a restricted facultatively methylotrophic bacterium Methylovorus sp. strain SS1
    • Seo, S. A. and Kim, Y. M. (1993) Isolation and characterization of a restricted facultatively methylotrophic bacterium Methylovorus sp. strain SS1. Kor. J. Microbiol. 31, 179-183.
    • (1993) Kor. J. Microbiol. , vol.31 , pp. 179-183
    • Seo, S.A.1    Kim, Y.M.2
  • 41
    • 0016154301 scopus 로고
    • The S'-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine, J. and Dalgarno, L. (1974) The S'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sci. USA 71, 1342-1346.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 43
    • 0020030003 scopus 로고
    • Evidence that the two Escherichia call groE morphogenetic gene products interact in vivo
    • Tilly, K. and Georgopoulos, C. (1982) Evidence that the two Escherichia call groE morphogenetic gene products interact in vivo. J. Bacteriol. 149, 1082-1088.
    • (1982) J. Bacteriol. , vol.149 , pp. 1082-1088
    • Tilly, K.1    Georgopoulos, C.2
  • 44
    • 0345483102 scopus 로고
    • Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis
    • Tilly, K., Murialdo, H. and Georgopoulos, C. (1981) Identification of a second Escherichia coli groE gene whose product is necessary for bacteriophage morphogenesis. Proc. Natl. Acad. Sci. USA 78, 1629-1633.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 1629-1633
    • Tilly, K.1    Murialdo, H.2    Georgopoulos, C.3
  • 45
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T. and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 46
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura, T., Nagai, H. and Mori, H. (1993) Regulation of the heat-shock response in bacteria. Annu. Rev. Microbiol. 47, 321-350.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 321-350
    • Yura, T.1    Nagai, H.2    Mori, H.3
  • 47
    • 0023683820 scopus 로고
    • Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor sigma 32
    • Zhou, Y. N., Kusukawa, N., Erickson, J. W., Gross, C. A. and Yura, T. (1988) Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor sigma 32. J. Bacteriol. 170, 3640-3649.
    • (1988) J. Bacteriol. , vol.170 , pp. 3640-3649
    • Zhou, Y.N.1    Kusukawa, N.2    Erickson, J.W.3    Gross, C.A.4    Yura, T.5
  • 48
    • 0028292919 scopus 로고
    • CIRCE, a novel heat shock element involved in regulation of heat shock operon dnaK of Bacillus subtilis
    • Zuber, U. and Schumann, W. (1994) CIRCE, a novel heat shock element involved in regulation of heat shock operon dnaK of Bacillus subtilis. J. Bacteriol. 176, 1359-1363.
    • (1994) J. Bacteriol. , vol.176 , pp. 1359-1363
    • Zuber, U.1    Schumann, W.2


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