메뉴 건너뛰기




Volumn 178, Issue 15, 1996, Pages 4611-4619

Cold shock stress-induced proteins in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN;

EID: 0029744180     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.15.4611-4619.1996     Document Type: Article
Times cited : (238)

References (64)
  • 1
    • 85035170574 scopus 로고    scopus 로고
    • Unpublished data
    • Antelmann, H. Unpublished data.
    • Antelmann, H.1
  • 3
    • 0026728335 scopus 로고
    • Streptomyces contain a 7.0 kDa cold shock like protein
    • Av-Gay, Y., Y. Aharonowitz, and G. Cohen. 1992. Streptomyces contain a 7.0 kDa cold shock like protein. Nucleic Acids Res. 20: 5478-5479.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5478-5479
    • Av-Gay, Y.1    Aharonowitz, Y.2    Cohen, G.3
  • 4
    • 85035163681 scopus 로고    scopus 로고
    • Berger, F., P. Potier, and P. Normand. 1995. EMBL/DDBJ accession no. L41167
    • Berger, F., P. Potier, and P. Normand. 1995. EMBL/DDBJ accession no. L41167.
  • 5
    • 0026623151 scopus 로고
    • Identification and characterization of FliY, a novel component of the Bacillus subtilis flagellar switch complex
    • Bischoff, D. S., M. D. Weinreich, and G. W. Ordal. 1992. Identification and characterization of FliY, a novel component of the Bacillus subtilis flagellar switch complex. J. Bacteriol. 174: 4017-4025.
    • (1992) J. Bacteriol. , vol.174 , pp. 4017-4025
    • Bischoff, D.S.1    Weinreich, M.D.2    Ordal, G.W.3
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification 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
  • 7
    • 0028609091 scopus 로고
    • Interaction of the main cold shock protein CS 7.4 (CspA) of Escherichia coli with the promoter region of hns
    • Brandi, A., C. L. Pon, and C. O. Gualerzi. 1994. Interaction of the main cold shock protein CS 7.4 (CspA) of Escherichia coli with the promoter region of hns. Biochimie 76: 1090-1098.
    • (1994) Biochimie , vol.76 , pp. 1090-1098
    • Brandi, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 8
    • 0025830893 scopus 로고
    • Characterization and sequence of the Escherichia coli stress-induced psp operon
    • Brissette, J. L., L. Weiner, T. L. Ripmaster, and P. Model. 1991 Characterization and sequence of the Escherichia coli stress-induced psp operon. J. Mol. Biol. 220: 35-48.
    • (1991) J. Mol. Biol. , vol.220 , pp. 35-48
    • Brissette, J.L.1    Weiner, L.2    Ripmaster, T.L.3    Model, P.4
  • 9
    • 0017888519 scopus 로고
    • Effects of low temperature on in vivo and in vitro protein synthesis in Escherichia coli and Pseudomonas fluorescent
    • Broeze, R. J., C. Solomon, and D. H. Pope. 1978. Effects of low temperature on in vivo and in vitro protein synthesis in Escherichia coli and Pseudomonas fluorescent. J. Bacteriol. 134: 861-874.
    • (1978) J. Bacteriol. , vol.134 , pp. 861-874
    • Broeze, R.J.1    Solomon, C.2    Pope, D.H.3
  • 10
    • 0024419052 scopus 로고
    • Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjecent genes homologous to uvrC and trx of Escherichia coli
    • Chen, N.-Y., J.-J. Zhang, and H. Paulus. 1989. Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjecent genes homologous to uvrC and trx of Escherichia coli. J. Gen. Microbiol. 135: 2931-2934.
    • (1989) J. Gen. Microbiol. , vol.135 , pp. 2931-2934
    • Chen, N.-Y.1    Zhang, J.-J.2    Paulus, H.3
  • 11
    • 0026760910 scopus 로고
    • Heat and cold shock protein synthesis in arctic and temperate strains of rhizohia
    • Cloutier, J., D. Prevost, P. Nadeau, and H. Antoun. 1992. Heat and cold shock protein synthesis in arctic and temperate strains of rhizohia. Appl. Environ. Microbiol. 58: 2846-2853.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 2846-2853
    • Cloutier, J.1    Prevost, D.2    Nadeau, P.3    Antoun, H.4
  • 12
    • 85035162033 scopus 로고    scopus 로고
    • Francis, K. P., C. E. D. Rees, and G. S. A. B. Stewart. 1995. EMBL/DDBJ accession no. X91789
    • Francis, K. P., C. E. D. Rees, and G. S. A. B. Stewart. 1995. EMBL/DDBJ accession no. X91789.
  • 13
    • 0028144747 scopus 로고
    • Responses to nutrient starvation in Pseudomonas putida KT2442: Two-dimensional electrophoretic analysis of starvation- And stress-induced proteins
    • Givskov, M., L. Eberl, and S. Molin. 1994. Responses to nutrient starvation in Pseudomonas putida KT2442: two-dimensional electrophoretic analysis of starvation- and stress-induced proteins. J. Bacteriol. 176: 4816-4824.
    • (1994) J. Bacteriol. , vol.176 , pp. 4816-4824
    • Givskov, M.1    Eberl, L.2    Molin, S.3
  • 14
    • 85035160151 scopus 로고    scopus 로고
    • Glaser, P., M. Ionescu, A. Vertes, M. Santana, F. Kunst, G. Rapoport, and A. Danchin. 1993. EMBL/GenBank accession no. Z28592
    • Glaser, P., M. Ionescu, A. Vertes, M. Santana, F. Kunst, G. Rapoport, and A. Danchin. 1993. EMBL/GenBank accession no. Z28592.
  • 15
    • 0028264505 scopus 로고
    • DNA supercoiling and thermal regulation of unsaturated fatty acid synthesis in Bacillus subtilis
    • Grau, R., D. Gardiol, G. C. Glikin, and D. de Mendoza. 1994. DNA supercoiling and thermal regulation of unsaturated fatty acid synthesis in Bacillus subtilis. Mol. Microbiol. 11: 933-941.
    • (1994) Mol. Microbiol. , vol.11 , pp. 933-941
    • Grau, R.1    Gardiol, D.2    Glikin, G.C.3    De Mendoza, D.4
  • 16
    • 0028012282 scopus 로고
    • The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- And CCAAT sequences in single-stranded oligonucleotides
    • Graumann, P., and M. A. Marahiel. 1994. The major cold shock protein of Bacillus subtilis CspB binds with high affinity to the ATTGG- and CCAAT sequences in single-stranded oligonucleotides. FEBS Lett. 338: 157-160.
    • (1994) FEBS Lett. , vol.338 , pp. 157-160
    • Graumann, P.1    Marahiel, M.A.2
  • 17
    • 0030131150 scopus 로고    scopus 로고
    • A case of convergent evolution of nucleic acid-binding modules
    • Graumann, P., and M. A. Marahiel. 1996, A case of convergent evolution of nucleic acid-binding modules. Bioessays 18: 309-315.
    • (1996) Bioessays , vol.18 , pp. 309-315
    • Graumann, P.1    Marahiel, M.A.2
  • 18
    • 0027509821 scopus 로고
    • Survival of hunger and stress-the role of rpoS in early stationary phase gene regulation in E. coli
    • Hengge-Aronis, R. 1993. Survival of hunger and stress-the role of rpoS in early stationary phase gene regulation in E. coli. Cell 72: 165-168.
    • (1993) Cell , vol.72 , pp. 165-168
    • Hengge-Aronis, R.1
  • 19
    • 0028217756 scopus 로고
    • Cloning and characterization of ppiB, a Bacillus subtilis gene which encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase
    • Herrler, M., H. Bang, and M. A. Marahiel. 1994. Cloning and characterization of ppiB, a Bacillus subtilis gene which encodes a cyclosporin A-sensitive peptidyl-prolyl cis-trans isomerase. Mol. Microbiol. 11: 1073-1083.
    • (1994) Mol. Microbiol. , vol.11 , pp. 1073-1083
    • Herrler, M.1    Bang, H.2    Marahiel, M.A.3
  • 20
    • 0020012835 scopus 로고
    • Purification and characterization of 30S ribosomal proteins from Bacillus subtilis: Correlation to Escherichia coli 30S proteins
    • Higo, K. I., E. Olaka, and S. Osawa. 1982. Purification and characterization of 30S ribosomal proteins from Bacillus subtilis: correlation to Escherichia coli 30S proteins. Mol. Gen. Genet. 185: 239-244.
    • (1982) Mol. Gen. Genet. , vol.185 , pp. 239-244
    • Higo, K.I.1    Olaka, E.2    Osawa, S.3
  • 21
    • 0026577548 scopus 로고
    • SpoVG sequence of Bacillus megaterium and Bacillus subtilis
    • Hudspeth, D. S. S., and P. S. Vary. 1992. SpoVG sequence of Bacillus megaterium and Bacillus subtilis. Biochim. Biophys. Acta 1130: 229-231.
    • (1992) Biochim. Biophys. Acta , vol.1130 , pp. 229-231
    • Hudspeth, D.S.S.1    Vary, P.S.2
  • 22
    • 0018956387 scopus 로고
    • The primary structure of Bacillus subtilis ribosomal protein B-19. Isolation and characterization of peptides and the complete amino acid sequence
    • Itoh, T., and B. Wittmann-Liebold. 1980. The primary structure of Bacillus subtilis ribosomal protein B-19. Isolation and characterization of peptides and the complete amino acid sequence. J. Biochem. 87: 1185-1198.
    • (1980) J. Biochem. , vol.87 , pp. 1185-1198
    • Itoh, T.1    Wittmann-Liebold, B.2
  • 23
    • 0026680453 scopus 로고
    • Function of a relaxed-like state following temperature downshifts in Escherichia coli
    • Jones, P. G., M. Cashel, G. Glaser, and F. C. Neidhardt. 1992. Function of a relaxed-like state following temperature downshifts in Escherichia coli. J. Bacteriol. 174: 3903-3914.
    • (1992) J. Bacteriol. , vol.174 , pp. 3903-3914
    • Jones, P.G.1    Cashel, M.2    Glaser, G.3    Neidhardt, F.C.4
  • 24
    • 0028363836 scopus 로고
    • The cold shock response - A hot topic
    • Jones, P. G., and M. Inouye. 1994. The cold shock response - a hot topic. Mol. Microbiol. 11: 811-818.
    • (1994) Mol. Microbiol. , vol.11 , pp. 811-818
    • Jones, P.G.1    Inouye, M.2
  • 25
    • 0026641172 scopus 로고
    • DNA gyrase, CS7.4, and the cold shock response in Escherichia coli
    • Jones, P. G., R. Krah, S. Tafuri, and A. P. Wolffe. 1992. DNA gyrase, CS7.4, and the cold shock response in Escherichia coli. J. Bacteriol. 174: 5798-5802.
    • (1992) J. Bacteriol. , vol.174 , pp. 5798-5802
    • Jones, P.G.1    Krah, R.2    Tafuri, S.3    Wolffe, A.P.4
  • 26
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperatures in Escherichia coli
    • Jones, P. G., R. A. Van Bogelen, and F. C. Neidhardt. 1987. Induction of proteins in response to low temperatures in Escherichia coli. J. Bacteriol. 169: 2092-2095.
    • (1987) J. Bacteriol. , vol.169 , pp. 2092-2095
    • Jones, P.G.1    Van Bogelen, R.A.2    Neidhardt, F.C.3
  • 27
    • 0026530785 scopus 로고
    • Analysis of genes involved in biosynthesis of the lantibiotic subtilin
    • Klein, C., C. Kaletta, N. Schnell, and K.-D. Entian. 1992. Analysis of genes involved in biosynthesis of the lantibiotic subtilin. Appl. Environ. Microbiol. 58: 132-142.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 132-142
    • Klein, C.1    Kaletta, C.2    Schnell, N.3    Entian, K.-D.4
  • 28
    • 0025790144 scopus 로고
    • Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS
    • La Teana, A., A. Brandi, M. Falconi, R. Spurion, C. Pon, and C. O. Gualerzi. 1991. Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS. Proc. Natl. Acad. Sci. USA 88: 10907-10911.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10907-10911
    • La Teana, A.1    Brandi, A.2    Falconi, M.3    Spurion, R.4    Pon, C.5    Gualerzi, C.O.6
  • 29
    • 85035164302 scopus 로고    scopus 로고
    • Law, R. M., and A. K. Bej. 1993. EMBL/DDBJ accession no. L23115
    • Law, R. M., and A. K. Bej. 1993. EMBL/DDBJ accession no. L23115.
  • 30
    • 0028339430 scopus 로고
    • Family of the major cold-shock protein, CspA (CS7.4), of Escherichia coli, whose members show a high sequence similarity with the eukaryotic Y-box binding proteins
    • Lee, S. J., A. Xie, W. Jiang, J.-P. Etchegaray, P. G. Jones, and M. Inouye. 1994. Family of the major cold-shock protein, CspA (CS7.4), of Escherichia coli, whose members show a high sequence similarity with the eukaryotic Y-box binding proteins. Mol. Microbiol. 11: 833-839.
    • (1994) Mol. Microbiol. , vol.11 , pp. 833-839
    • Lee, S.J.1    Xie, A.2    Jiang, W.3    Etchegaray, J.-P.4    Jones, P.G.5    Inouye, M.6
  • 31
    • 0028937740 scopus 로고
    • Induction of cold shock proteins in Bacillus subtilis
    • Lottering, E. A., and U. N. Streips. 1995. Induction of cold shock proteins in Bacillus subtilis. Curr. Microbiol. 30: 193-199.
    • (1995) Curr. Microbiol. , vol.30 , pp. 193-199
    • Lottering, E.A.1    Streips, U.N.2
  • 32
    • 0023127370 scopus 로고
    • Heavy riboflavin synthase of Bacillus subtilis. Primary structure of the beta subunit
    • Ludwig, H. C., F. Lottspeich, A. Henschen, R. Ladenstein, and A. Bacher. 1987. Heavy riboflavin synthase of Bacillus subtilis. Primary structure of the beta subunit. J. Biol. Chem. 262: 1016-1021.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1016-1021
    • Ludwig, H.C.1    Lottspeich, F.2    Henschen, A.3    Ladenstein, R.4    Bacher, A.5
  • 33
    • 0028897341 scopus 로고
    • The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter
    • MacDonald, G. H., Y. Itoh-Lindstrom, and J. P.-Y. Ting. 1995. The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter. J. Biol. Chem. 270: 3527-3533.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3527-3533
    • MacDonald, G.H.1    Itoh-Lindstrom, Y.2    Ting, J.P.-Y.3
  • 34
    • 0028593677 scopus 로고
    • Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis
    • Makhatadze, G. I., and M. A. Marahiel. 1994. Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. Protein Sci. 3: 2144-2147.
    • (1994) Protein Sci. , vol.3 , pp. 2144-2147
    • Makhatadze, G.I.1    Marahiel, M.A.2
  • 36
    • 0026772542 scopus 로고
    • Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis
    • Mitchell, C., P. W. Morris, and J. C. Vary. 1992. Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis. J. Bacteriol. 174: 2474-2477.
    • (1992) J. Bacteriol. , vol.174 , pp. 2474-2477
    • Mitchell, C.1    Morris, P.W.2    Vary, J.C.3
  • 37
    • 0026778118 scopus 로고
    • Amino acid sequence of several Bacillus subtilis proteins modified by apparent guanylylation
    • Mitchell, C., P. W. Morris, and J. C. Vary. 1992. Amino acid sequence of several Bacillus subtilis proteins modified by apparent guanylylation. Mol. Microbiol. 6: 1579-1581.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1579-1581
    • Mitchell, C.1    Morris, P.W.2    Vary, J.C.3
  • 38
    • 0028234777 scopus 로고
    • Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: Identification of a binding epitope for DNA
    • Newkirk, K., W. Feng, W. Jiang, R. Tejero, S. D. Emerson, M. Inouye, and G. T. Montelione. 1994. Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA. Proc. Natl. Acad. Sci. USA 91: 5114-5118.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5114-5118
    • Newkirk, K.1    Feng, W.2    Jiang, W.3    Tejero, R.4    Emerson, S.D.5    Inouye, M.6    Montelione, G.T.7
  • 39
    • 0028700721 scopus 로고
    • Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin
    • Ogasawara, N., S. Nakai, and H. Yoshikawa. 1994. Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin. DNA Res. 1: 1-14.
    • (1994) DNA Res. , vol.1 , pp. 1-14
    • Ogasawara, N.1    Nakai, S.2    Yoshikawa, H.3
  • 41
    • 0028957034 scopus 로고    scopus 로고
    • The Escherichia coli ribosomal RNA leader nut region interacts specifically with mature 16S RNA
    • Pardon, B., and R. Wagner. The Escherichia coli ribosomal RNA leader nut region interacts specifically with mature 16S RNA. Nucleic Acids Res. 23: : 932-941.
    • Nucleic Acids Res. , vol.23 , pp. 932-941
    • Pardon, B.1    Wagner, R.2
  • 42
    • 0028942797 scopus 로고
    • Analysis of heat and cold shock proteins in Listeria by two-dimensional electrophoresis
    • Phan-Thanh, L., and T. Gormon. 1995. Analysis of heat and cold shock proteins in Listeria by two-dimensional electrophoresis. Electrophoresis 16: 444-450.
    • (1995) Electrophoresis , vol.16 , pp. 444-450
    • Phan-Thanh, L.1    Gormon, T.2
  • 43
    • 0028047396 scopus 로고
    • Occurrence and expression of cspA, a cold shock gene, in Antarctic psychotrophic bacteria
    • Ray, M. K., T. Sitaramamma, S. Ghandhi, and S. Shivaji. 1994. Occurrence and expression of cspA, a cold shock gene, in Antarctic psychotrophic bacteria. FEMS Microbiol. Lett. 116: 55-60.
    • (1994) FEMS Microbiol. Lett. , vol.116 , pp. 55-60
    • Ray, M.K.1    Sitaramamma, T.2    Ghandhi, S.3    Shivaji, S.4
  • 44
    • 0029077343 scopus 로고
    • An agarosc-based gel-concentration system for microsequence and mass spectrometric characterization of proteins previously purified in polyacrylamide gels starting at low picomole levels
    • Rider, M. H., M. Puype, J. Van Damme, K. Gevaert, S, De Boeck, J. D'Alayer, H. H. Rasmussen, J. E. Celis, and J. Vanderkerckhove. 1995. An agarosc-based gel-concentration system for microsequence and mass spectrometric characterization of proteins previously purified in polyacrylamide gels starting at low picomole levels. Eur. J. Biochem. 230: 258-256.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 258-1256
    • Rider, M.H.1    Puype, M.2    Van Damme, J.3    Gevaert, K.4    De Boeck, S.5    Alayer, J.D.6    Rasmussen, H.H.7    Celis, J.E.8    Vanderkerckhove, J.9
  • 46
    • 0028306109 scopus 로고
    • Crystal structure of CspA, the major cold shock protein of Escherichia coli
    • Schindelin, H., W. Jiang, M. Inouye, and U. Heinemann. 1994. Crystal structure of CspA, the major cold shock protein of Escherichia coli. Proc. Natl. Acad. Sci. USA 91: 5119-5123.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5119-5123
    • Schindelin, H.1    Jiang, W.2    Inouye, M.3    Heinemann, U.4
  • 47
    • 0027296211 scopus 로고
    • Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
    • Schindelin, H., M. A. Marahiel, and U. Heinemann. 1993. Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature (London) 364: 164-167.
    • (1993) Nature (London) , vol.364 , pp. 164-167
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 49
    • 85035162228 scopus 로고    scopus 로고
    • Unpublished data
    • 47a.Schmidt, A., et al. Unpublished data.
    • Schmidt, A.1
  • 50
    • 0026776431 scopus 로고
    • Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis
    • Schmidt, A., M. Schiesswohl, V. Völker, M. Hecker, and W. Schumann. 1992. Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis. J. Bacteriol. 174: 3993-3999.
    • (1992) J. Bacteriol. , vol.174 , pp. 3993-3999
    • Schmidt, A.1    Schiesswohl, M.2    Völker, V.3    Hecker, M.4    Schumann, W.5
  • 52
    • 0029078286 scopus 로고
    • Mutational analysis of the putative nucleic acid binding surface of the cold shock domain, CspB, revealed an essential role of aromatic and basic residues in binding single-stranded DNA containing the Y-box motif
    • Schröder, K., P. Graumann, A. Schnuchel, T. A. Holak, and M. A. Marahiel. 1995. Mutational analysis of the putative nucleic acid binding surface of the cold shock domain, CspB, revealed an essential role of aromatic and basic residues in binding single-stranded DNA containing the Y-box motif. Mol. Microbiol. 16: 699-708.
    • (1995) Mol. Microbiol. , vol.16 , pp. 699-708
    • Schröder, K.1    Graumann, P.2    Schnuchel, A.3    Holak, T.A.4    Marahiel, M.A.5
  • 53
    • 0027723741 scopus 로고
    • Mapping of the Bacillus subtilis cspB gene and cloning of its homologs in thermophilic, mesophilic and psychotropic bacilli
    • Schröder, K., P. Zuber, G. Willimsky, B. Wagner and M. A. Marahiel. 1993. Mapping of the Bacillus subtilis cspB gene and cloning of its homologs in thermophilic, mesophilic and psychotropic bacilli. Gene 136: 277-280.
    • (1993) Gene , vol.136 , pp. 277-280
    • Schröder, K.1    Zuber, P.2    Willimsky, G.3    Wagner, B.4    Marahiel, M.A.5
  • 54
    • 0024076474 scopus 로고
    • Complete sequence and transcriptional analysts of the spoof region of the Bacillus subtilis chromosome
    • Trach, K., J. W. Charman, P. Piggot, D. LeCoq, and J. D. Hoch. 1988. Complete sequence and transcriptional analysts of the spoOF region of the Bacillus subtilis chromosome. J. Bacteriol. 170: 4194-4208.
    • (1988) J. Bacteriol. , vol.170 , pp. 4194-4208
    • Trach, K.1    Charman, J.W.2    Piggot, P.3    LeCoq, D.4    Hoch, J.D.5
  • 55
    • 0025328743 scopus 로고
    • Ribosomes as sensors of heat and cold shock in Escherichia coli
    • Van Bogelen, R., and F. C. Neidhardt. 1990. Ribosomes as sensors of heat and cold shock in Escherichia coli. Proc. Natl. Acad. Sci. USA 87: 5589-5593.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5589-5593
    • Van Bogelen, R.1    Neidhardt, F.C.2
  • 56
    • 85035168532 scopus 로고    scopus 로고
    • Vandeyar, M. A., P. B. Vander Horn, J. A. Rafael, J. A. Grandoni, and S. A. Zahler. 1992. EMBL/Genbank/DDBJ data hanks (P37253)
    • Vandeyar, M. A., P. B. Vander Horn, J. A. Rafael, J. A. Grandoni, and S. A. Zahler. 1992. EMBL/Genbank/DDBJ data hanks (P37253).
  • 57
    • 0024564613 scopus 로고
    • Sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from Bacillus subtilis
    • Viane, A., and P. Dhaese. 1989. Sequence of the glyceraldehyde-3-phosphate dehydrogenase gene from Bacillus subtilis. Nucleic Acids Res. 17: 1251.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 1251
    • Viane, A.1    Dhaese, P.2
  • 60
    • 0027058752 scopus 로고
    • Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium
    • Whyte, L. G., and W. E. Inniss. 1992. Cold shock proteins and cold acclimation proteins in a psychrotrophic bacterium. Can. J. Microbiol. 38: 1281-1285.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 1281-1285
    • Whyte, L.G.1    Inniss, W.E.2
  • 61
    • 0026648953 scopus 로고
    • Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting viability at low temperatures
    • Willimsky, G., H. Bang, G. Fischer, and M. A. Marahiel. 1992 Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting viability at low temperatures. J. Bacteriol. 174: 6326-6335.
    • (1992) J. Bacteriol. , vol.174 , pp. 6326-6335
    • Willimsky, G.1    Bang, H.2    Fischer, G.3    Marahiel, M.A.4
  • 62
    • 0025910398 scopus 로고
    • Temperature-induced protein synthesis in Bacillus stearothermophilus NUB36
    • Wu, L., and N. E. Welker. 1991. Temperature-induced protein synthesis in Bacillus stearothermophilus NUB36. J. Bacteriol. 173: 4889-4892.
    • (1991) J. Bacteriol. , vol.173 , pp. 4889-4892
    • Wu, L.1    Welker, N.E.2
  • 63
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura, T., H. Nagai, and H. Mori. 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
  • 64
    • 0013577479 scopus 로고
    • Localizing the site of spoO-dependent regulation in the spoVG promoter of Bacillus subtilis
    • J. A. Hoch and P. Setlow (ed.), American Society for Microbiology, Washington, D.C.
    • Zuber, P. 1985. Localizing the site of spoO-dependent regulation in the spoVG promoter of Bacillus subtilis, p. 149-156. In J. A. Hoch and P. Setlow (ed.), Molecular biology of microbial differentiation. American Society for Microbiology, Washington, D.C.
    • (1985) Molecular Biology of Microbial Differentiation , pp. 149-156
    • Zuber, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.