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Volumn 30, Issue 5, 2006, Pages 734-759

How high G+C Gram-positive bacteria and in particular bifidobacteria cope with heat stress: Protein players and regulators

Author keywords

Actinobacteria; Bifidobacteria; Gene regulation; Stress response

Indexed keywords

BACTERIAL PROTEIN; CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 100; HEAT SHOCK PROTEIN 60; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; NUCLEOTIDE; PROTEIN DNAK; PROTEINASE; REGULATOR PROTEIN; SIGMA FACTOR;

EID: 33746933405     PISSN: 01686445     EISSN: 15746976     Source Type: Journal    
DOI: 10.1111/j.1574-6976.2006.00031.x     Document Type: Review
Times cited : (52)

References (151)
  • 1
    • 0033568606 scopus 로고    scopus 로고
    • The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor
    • Ades SE, Connolly LE, Alba BM & Gross CA (1999) The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor. Genes Dev 13: 2449-2461.
    • (1999) Genes Dev , vol.13 , pp. 2449-2461
    • Ades, S.E.1    Connolly, L.E.2    Alba, B.M.3    Gross, C.A.4
  • 2
    • 0034933064 scopus 로고    scopus 로고
    • DegS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity
    • Alba BM, Zhong HJ, Pelayo JC & Gross CA (2001) degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity. Mol Microbiol 40: 1323-1333.
    • (2001) Mol Microbiol , vol.40 , pp. 1323-1333
    • Alba, B.M.1    Zhong, H.J.2    Pelayo, J.C.3    Gross, C.A.4
  • 3
    • 15844379133 scopus 로고    scopus 로고
    • Diverse roles for HspR in Campylobacter jejuni revealed by the proteome, transcriptome and phenotypic characterization of an hspR mutant
    • Andersen MT, Brondsted L, Pearson BM, Mulholland F, Parker M, Pin C, Wells JM & Ingmer H (2005) Diverse roles for HspR in Campylobacter jejuni revealed by the proteome, transcriptome and phenotypic characterization of an hspR mutant. Microbiology 151: 905-915.
    • (2005) Microbiology , vol.151 , pp. 905-915
    • Andersen, M.T.1    Brondsted, L.2    Pearson, B.M.3    Mulholland, F.4    Parker, M.5    Pin, C.6    Wells, J.M.7    Ingmer, H.8
  • 4
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181: 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 5
    • 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 & Fischer HM (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
  • 6
    • 0024538993 scopus 로고
    • Cloning and sequence analysis of the 10 kDa antigen gene of Mycobacterium tuberculosis
    • Baird PN, Hall LM & Coates AR (1989) Cloning and sequence analysis of the 10 kDa antigen gene of Mycobacterium tuberculosis. J Gen Microbiol 135: 931-939.
    • (1989) J Gen Microbiol , vol.135 , pp. 931-939
    • Baird, P.N.1    Hall, L.M.2    Coates, A.R.3
  • 7
    • 13244282994 scopus 로고    scopus 로고
    • Heat shock proteome analysis of wild-type Corynebacterium glutamicum ATCC 13032 and a spontaneous mutant lacking GroEL1, a dispensable chaperone
    • Barreiro C, Gonzalez-Lavado E, Brand S, Tauch A & Martin JF (2005) Heat shock proteome analysis of wild-type Corynebacterium glutamicum ATCC 13032 and a spontaneous mutant lacking GroEL1, a dispensable chaperone. J Bacteriol 187: 884-889.
    • (2005) J Bacteriol , vol.187 , pp. 884-889
    • Barreiro, C.1    Gonzalez-Lavado, E.2    Brand, S.3    Tauch, A.4    Martin, J.F.5
  • 8
    • 2342606509 scopus 로고    scopus 로고
    • ClgR, a novel regulator of clp and lon expression in Streptomyces
    • Bellier A & Mazodier P (2004) ClgR, a novel regulator of clp and lon expression in Streptomyces. J Bacteriol 186: 3238-3248.
    • (2004) J Bacteriol , vol.186 , pp. 3238-3248
    • Bellier, A.1    Mazodier, P.2
  • 9
    • 0037046560 scopus 로고    scopus 로고
    • Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)
    • Bentley SD, Chater KF, Cerdeno-Tarraga AM, et al. (2002) Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature 417: 141-147.
    • (2002) Nature , vol.417 , pp. 141-147
    • Bentley, S.D.1    Chater, K.F.2    Cerdeno-Tarraga, A.M.3
  • 10
    • 0037460735 scopus 로고    scopus 로고
    • Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei
    • Bentley SD, Maiwald M, Murphy LD, et al. (2003) Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei. Lancet 361: 637-644.
    • (2003) Lancet , vol.361 , pp. 637-644
    • Bentley, S.D.1    Maiwald, M.2    Murphy, L.D.3
  • 11
    • 0028805520 scopus 로고
    • Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase
    • Blaszczak A, Zylicz M, Georgopoulos C & Liberek K (1995) Both ambient temperature and the DnaK chaperone machine modulate the heat shock response in Escherichia coli by regulating the switch between sigma 70 and sigma 32 factors assembled with RNA polymerase. Embo J 14: 5085-5093.
    • (1995) Embo J , vol.14 , pp. 5085-5093
    • Blaszczak, A.1    Zylicz, M.2    Georgopoulos, C.3    Liberek, K.4
  • 16
    • 0029161644 scopus 로고
    • The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock protein which binds to the promoter region of the operon
    • Bucca G, Ferina G, Puglia AM & Smith CP (1995) The dnaK operon of Streptomyces coelicolor encodes a novel heat-shock protein which binds to the promoter region of the operon. Mol Microbiol 17: 663-674.
    • (1995) Mol Microbiol , vol.17 , pp. 663-674
    • Bucca, G.1    Ferina, G.2    Puglia, A.M.3    Smith, C.P.4
  • 17
    • 0030883870 scopus 로고    scopus 로고
    • Regulation of the dnaK operon of Streptomyces coelicolor A3(2) is governed by HspR, an autoregulatory repressor protein
    • Bucca G, Hindle Z & Smith CP (1997) Regulation of the dnaK operon of Streptomyces coelicolor A3(2) is governed by HspR, an autoregulatory repressor protein. J Bacteriol 179: 5999-6004.
    • (1997) J Bacteriol , vol.179 , pp. 5999-6004
    • Bucca, G.1    Hindle, Z.2    Smith, C.P.3
  • 18
    • 0034530509 scopus 로고    scopus 로고
    • The HspR regulon of Streptomyces coelicolor: A role for the DnaK chaperone as a transcriptional co-repressordagger
    • Bucca G, Brassington AM, Schonfeld HJ & Smith CP (2000) The HspR regulon of Streptomyces coelicolor: a role for the DnaK chaperone as a transcriptional co-repressordagger. Mol Microbiol 38: 1093-1103.
    • (2000) Mol Microbiol , vol.38 , pp. 1093-1103
    • Bucca, G.1    Brassington, A.M.2    Schonfeld, H.J.3    Smith, C.P.4
  • 19
    • 0141818925 scopus 로고    scopus 로고
    • Negative feedback regulation of dnaK, clpB and lon expression by the DnaK chaperone machine in Streptomyces coelicolor, identified by transcriptome and in vivo DnaK-depletion analysis
    • Bucca G, Brassington AM, Hotchkiss G, Mersinias V & Smith CP (2003) Negative feedback regulation of dnaK, clpB and lon expression by the DnaK chaperone machine in Streptomyces coelicolor, identified by transcriptome and in vivo DnaK-depletion analysis. Mol Microbiol 50: 153-166.
    • (2003) Mol Microbiol , vol.50 , pp. 153-166
    • Bucca, G.1    Brassington, A.M.2    Hotchkiss, G.3    Mersinias, V.4    Smith, C.P.5
  • 20
    • 0027319272 scopus 로고
    • Regulation of the Escherichia coli heat-shock response
    • Bukau B (1993) Regulation of the Escherichia coli heat-shock response. Mol Microbiol 9: 671-680.
    • (1993) Mol Microbiol , vol.9 , pp. 671-680
    • Bukau, B.1
  • 21
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B & Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 22
    • 0034646515 scopus 로고    scopus 로고
    • Getting newly synthesized proteins into shape
    • Bukau B, Deuerling E, Pfund C & Craig EA (2000) Getting newly synthesized proteins into shape. Cell 101: 119-122.
    • (2000) Cell , vol.101 , pp. 119-122
    • Bukau, B.1    Deuerling, E.2    Pfund, C.3    Craig, E.A.4
  • 23
    • 0032698634 scopus 로고    scopus 로고
    • Transcription activation by catabolite activator protein (CAP)
    • Busby S & Ebright RH (1999) Transcription activation by catabolite activator protein (CAP). J Mol Biol 293: 199-213.
    • (1999) J Mol Biol , vol.293 , pp. 199-213
    • Busby, S.1    Ebright, R.H.2
  • 24
    • 0028903455 scopus 로고
    • The expanding small heat-shock protein family, and structure predictions of the conserved ́alpha-crystallin domain"
    • Caspers GJ, Leunissen JA & de Jong WW (1995) The expanding small heat-shock protein family, and structure predictions of the conserved ́alpha-crystallin domain". J Mol Evol 40: 238-248.
    • (1995) J Mol Evol , vol.40 , pp. 238-248
    • Caspers, G.J.1    Leunissen, J.A.2    De Jong, W.W.3
  • 25
    • 10744229660 scopus 로고    scopus 로고
    • The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129
    • Cerdeno-Tarraga AM, Efstratiou A, Dover LG, et al. (2003) The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129. Nucleic Acids Res 31: 6516-6523.
    • (2003) Nucleic Acids Res , vol.31 , pp. 6516-6523
    • Cerdeno-Tarraga, A.M.1    Efstratiou, A.2    Dover, L.G.3
  • 26
    • 0030002946 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation
    • Chang Z, Primm TP, Jakana J, Lee IH, Serysheva I, Chiu W, Gilbert HF & Quiocho FA (1996) Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation. J Biol Chem 271: 7218-7223.
    • (1996) J Biol Chem , vol.271 , pp. 7218-7223
    • Chang, Z.1    Primm, T.P.2    Jakana, J.3    Lee, I.H.4    Serysheva, I.5    Chiu, W.6    Gilbert, H.F.7    Quiocho, F.A.8
  • 27
    • 0033805703 scopus 로고    scopus 로고
    • Construction and characterization of a Mycobacterium tuberculosis mutant lacking the alternate sigma factor gene, sigF
    • Chen P, Ruiz RE, Li Q, Silver RF & Bishai WR (2000) Construction and characterization of a Mycobacterium tuberculosis mutant lacking the alternate sigma factor gene, sigF. Infect Immun 68: 5575-5580.
    • (2000) Infect Immun , vol.68 , pp. 5575-5580
    • Chen, P.1    Ruiz, R.E.2    Li, Q.3    Silver, R.F.4    Bishai, W.R.5
  • 28
    • 0033971399 scopus 로고    scopus 로고
    • A developmentally regulated catalase required for proper differentiation and osmoprotection of Streptomyces coelicolor
    • Cho YH, Lee EJ & Roe JH (2000) A developmentally regulated catalase required for proper differentiation and osmoprotection of Streptomyces coelicolor. Mol Microbiol 35: 150-160.
    • (2000) Mol Microbiol , vol.35 , pp. 150-160
    • Cho, Y.H.1    Lee, E.J.2    Roe, J.H.3
  • 29
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole ST, Brosch R, Parkhill J, et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3
  • 30
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • Cupp-Vickery JR, Peterson JC, Ta DT & Vickery LE (2004) Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. J Mol Biol 342: 1265-1278.
    • (2004) J Mol Biol , vol.342 , pp. 1265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 31
    • 0032958485 scopus 로고    scopus 로고
    • Alteration of the synthesis of the Clp ATP-dependent protease affects morphological and physiological differentiation in Streptomyces
    • de Crecy-Lagard V, Servant-Moisson P, Viala J, Grandvalet C & Mazodier P (1999) Alteration of the synthesis of the Clp ATP-dependent protease affects morphological and physiological differentiation in Streptomyces. Mol Microbiol 32: 505-517.
    • (1999) Mol Microbiol , vol.32 , pp. 505-517
    • De Crecy-Lagard, V.1    Servant-Moisson, P.2    Viala, J.3    Grandvalet, C.4    Mazodier, P.5
  • 32
    • 0029981245 scopus 로고    scopus 로고
    • A stationary-phase stress-response sigma factor from Mycobacterium tuberculosis
    • DeMaio J, Zhang Y, Ko C, Young DB & Bishai WR (1996) A stationary-phase stress-response sigma factor from Mycobacterium tuberculosis. Proc Natl Acad Sci US A 93: 2790-2794.
    • (1996) Proc Natl Acad Sci US A , vol.93 , pp. 2790-2794
    • DeMaio, J.1    Zhang, Y.2    Ko, C.3    Young, D.B.4    Bishai, W.R.5
  • 33
    • 0032921346 scopus 로고    scopus 로고
    • CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria
    • Derre I, Rapoport G & Msadek T (1999) CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in gram-positive bacteria. Mol Microbiol 31: 117-131.
    • (1999) Mol Microbiol , vol.31 , pp. 117-131
    • Derre, I.1    Rapoport, G.2    Msadek, T.3
  • 34
    • 0033549770 scopus 로고    scopus 로고
    • Trigger factor and DnaK cooperate in folding of newly synthesized proteins
    • Deuerling E, Schulze-Specking A, Tomoyasu T, Mogk A & Bukau B (1999) Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400: 693-696.
    • (1999) Nature , vol.400 , pp. 693-696
    • Deuerling, E.1    Schulze-Specking, A.2    Tomoyasu, T.3    Mogk, A.4    Bukau, B.5
  • 35
    • 27844611623 scopus 로고
    • Culture conditions promoting dispersed growth and biphasic production of actinorhodin in shaken cultures of Streptomyces coelicolor A3(2)
    • Doull JL & Vining LC (1989) Culture conditions promoting dispersed growth and biphasic production of actinorhodin in shaken cultures of Streptomyces coelicolor A3(2). FEMS Microbiol Lett 53: 265-268.
    • (1989) FEMS Microbiol Lett , vol.53 , pp. 265-268
    • Doull, J.L.1    Vining, L.C.2
  • 37
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis J (1987) Proteins as molecular chaperones. Nature 328: 378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 38
    • 1942519868 scopus 로고    scopus 로고
    • clpC and clpP1P2 gene expression in Corynebacterium glutamicum is controlled by a regulatory network involving the transcriptional regulators ClgR and HspR as well as the ECF sigma factor sigmaH
    • Engels S, Schweitzer JE, Ludwig C, Bott M & Schaffer S (2004) clpC and clpP1P2 gene expression in Corynebacterium glutamicum is controlled by a regulatory network involving the transcriptional regulators ClgR and HspR as well as the ECF sigma factor sigmaH. Mol Microbiol 52: 285-302.
    • (2004) Mol Microbiol , vol.52 , pp. 285-302
    • Engels, S.1    Schweitzer, J.E.2    Ludwig, C.3    Bott, M.4    Schaffer, S.5
  • 39
    • 22144447873 scopus 로고    scopus 로고
    • The transcriptional activator ClgR controls transcription of genes involved in proteolysis and DNA repair in Corynebacterium glutamicum
    • Engels S, Ludwig C, Schweitzer JE, Mack C, Bott M & Schaffer S (2005) The transcriptional activator ClgR controls transcription of genes involved in proteolysis and DNA repair in Corynebacterium glutamicum. Mol Microbiol 57: 576-591.
    • (2005) Mol Microbiol , vol.57 , pp. 576-591
    • Engels, S.1    Ludwig, C.2    Schweitzer, J.E.3    Mack, C.4    Bott, M.5    Schaffer, S.6
  • 40
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt KL, Hendrick JP, Houry WA & Hartl FU (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    Hartl, F.U.4
  • 41
    • 0032779309 scopus 로고    scopus 로고
    • A mycobacterial extracytoplasmic sigma factor involved in survival following heat shock and oxidative stress
    • Fernandes ND, Wu QL, Kong D, Puyang X, Garg S & Husson RN (1999) A mycobacterial extracytoplasmic sigma factor involved in survival following heat shock and oxidative stress. J Bacteriol 181: 4266-4274.
    • (1999) J Bacteriol , vol.181 , pp. 4266-4274
    • Fernandes, N.D.1    Wu, Q.L.2    Kong, D.3    Puyang, X.4    Garg, S.5    Husson, R.N.6
  • 42
    • 0036777599 scopus 로고    scopus 로고
    • Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains
    • Fleischmann RD, Alland D, Eisen JA, et al. (2002) Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains. J Bacteriol 184: 5479-5490.
    • (2002) J Bacteriol , vol.184 , pp. 5479-5490
    • Fleischmann, R.D.1    Alland, D.2    Eisen, J.A.3
  • 43
    • 0035929156 scopus 로고    scopus 로고
    • Crystal structure of chaperonin-60 from Paracoccus denitrificans
    • Fukami TA, Yohda M, Taguchi H, Yoshida M & Miki K (2001) Crystal structure of chaperonin-60 from Paracoccus denitrificans. J Mol Biol 312: 501-509.
    • (2001) J Mol Biol , vol.312 , pp. 501-509
    • Fukami, T.A.1    Yohda, M.2    Taguchi, H.3    Yoshida, M.4    Miki, K.5
  • 44
    • 0037596510 scopus 로고    scopus 로고
    • The complete genome sequence of Mycobacterium bovis
    • Garnier T, Eiglmeier K, Camus JC, et al. (2003) The complete genome sequence of Mycobacterium bovis. Proc Natl Acad Sci USA 100: 7877-7882.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7877-7882
    • Garnier, T.1    Eiglmeier, K.2    Camus, J.C.3
  • 45
    • 0026074372 scopus 로고
    • The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein
    • Gaur NK, Oppenheim J & Smith I (1991) The Bacillus subtilis sin gene, a regulator of alternate developmental processes, codes for a DNA-binding protein. J Bacteriol 173: 678-686.
    • (1991) J Bacteriol , vol.173 , pp. 678-686
    • Gaur, N.K.1    Oppenheim, J.2    Smith, I.3
  • 46
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T & Bukau B (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci U S A 96: 13732-13737.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 47
    • 0031398423 scopus 로고    scopus 로고
    • Sigma factors of Mycobacterium tuberculosis
    • Gomez JE, Chen JM & Bishai WR (1997) Sigma factors of Mycobacterium tuberculosis. Tuber Lung Dis 78: 175-183.
    • (1997) Tuber Lung Dis , vol.78 , pp. 175-183
    • Gomez, J.E.1    Chen, J.M.2    Bishai, W.R.3
  • 48
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S (1996) Proteases and their targets in Escherichia coli. Annu Rev Genet 30: 465-506.
    • (1996) Annu Rev Genet , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 49
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman S, Wickner S & Maurizi MR (1997) Protein quality control: triage by chaperones and proteases. Genes Dev 11: 815-823.
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 50
    • 0032079329 scopus 로고    scopus 로고
    • The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
    • Gottesman S, Roche E, Zhou Y & Sauer RT (1998) The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system. Genes Dev 12: 1338-1347.
    • (1998) Genes Dev , vol.12 , pp. 1338-1347
    • Gottesman, S.1    Roche, E.2    Zhou, Y.3    Sauer, R.T.4
  • 51
    • 0031022299 scopus 로고    scopus 로고
    • Disruption of hspR, the repressor gene of the dnaK operon in Streptomyces albus G
    • Grandvalet C, Servant P & Mazodier P (1997) Disruption of hspR, the repressor gene of the dnaK operon in Streptomyces albus G. Mol Microbiol 23: 77-84.
    • (1997) Mol Microbiol , vol.23 , pp. 77-84
    • Grandvalet, C.1    Servant, P.2    Mazodier, P.3
  • 52
    • 0031714922 scopus 로고    scopus 로고
    • A, encoding the repressor of the groEL genes in Streptomyces albus G, is associated with a second dnaJ gene
    • Grandvalet C, Rapoport G & Mazodier P (1998) hrcA, encoding the repressor of the groEL genes in Streptomyces albus G, is associated with a second dnaJ gene. J Bacteriol 180: 5129-5134.
    • (1998) J Bacteriol , vol.180 , pp. 5129-5134
    • Grandvalet, C.1    Rapoport, G.2    Mazodier, P.3
  • 53
    • 0032524297 scopus 로고    scopus 로고
    • Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP
    • Grimaud R, Kessel M, Beuron F, Steven AC & Maurizi MR (1998) Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP. J Biol Chem 273: 12476-12481.
    • (1998) J Biol Chem , vol.273 , pp. 12476-12481
    • Grimaud, R.1    Kessel, M.2    Beuron, F.3    Steven, A.C.4    Maurizi, M.R.5
  • 55
    • 0025310356 scopus 로고
    • DNA recognition by proteins with the helix-turn-helix motif
    • Harrison SC & Aggarwal AK (1990) DNA recognition by proteins with the helix-turn-helix motif. Annu Rev Biochem 59: 933-969.
    • (1990) Annu Rev Biochem , vol.59 , pp. 933-969
    • Harrison, S.C.1    Aggarwal, A.K.2
  • 56
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F & Kuriyan J (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276: 431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 57
    • 0031679433 scopus 로고    scopus 로고
    • Non-specific, general and multiple stress resistance of growth-restricted Bacillus subtilis cells by the expression of the sigmaB regulon
    • Hecker M & Volker U (1998) Non-specific, general and multiple stress resistance of growth-restricted Bacillus subtilis cells by the expression of the sigmaB regulon. Mol Microbiol 29: 1129-1136.
    • (1998) Mol Microbiol , vol.29 , pp. 1129-1136
    • Hecker, M.1    Volker, U.2
  • 58
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker M, Schumann W & 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
  • 59
    • 0035905808 scopus 로고    scopus 로고
    • Crystal structure of the transcription activator BmrR bound to DNA and a drug
    • Heldwein EE & Brennan RG (2001) Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature 409: 378-382.
    • (2001) Nature , vol.409 , pp. 378-382
    • Heldwein, E.E.1    Brennan, R.G.2
  • 60
    • 0035985580 scopus 로고    scopus 로고
    • The extracytoplasmic function (ECF) sigma factors
    • Helmann JD (2002) The extracytoplasmic function (ECF) sigma factors. Adv Microb Physiol 46: 47-110.
    • (2002) Adv Microb Physiol , vol.46 , pp. 47-110
    • Helmann, J.D.1
  • 62
  • 63
    • 0033909787 scopus 로고    scopus 로고
    • Transcriptional analysis of major heat shock genes of Helicobacter pylori
    • Homuth G, Domm S, Kleiner D & Schumann W (2000) Transcriptional analysis of major heat shock genes of Helicobacter pylori. J Bacteriol 182: 4257-4263.
    • (2000) J Bacteriol , vol.182 , pp. 4257-4263
    • Homuth, G.1    Domm, S.2    Kleiner, D.3    Schumann, W.4
  • 64
    • 0031945917 scopus 로고    scopus 로고
    • The thermosome: Chaperonin with a built-in lid
    • Horwich AL & Saibil HR (1998) The thermosome: chaperonin with a built-in lid. Nat Struct Biol 5: 333-336.
    • (1998) Nat Struct Biol , vol.5 , pp. 333-336
    • Horwich, A.L.1    Saibil, H.R.2
  • 66
    • 0042162924 scopus 로고    scopus 로고
    • The Corynebacterium glutamicum genome: Features and impacts on biotechnological processes
    • Ikeda M & Nakagawa S (2003) The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl Microbiol Biotechnol 62: 99-109.
    • (2003) Appl Microbiol Biotechnol , vol.62 , pp. 99-109
    • Ikeda, M.1    Nakagawa, S.2
  • 69
    • 0027391629 scopus 로고
    • Small heat shock proteins are molecular chaperones
    • Jakob U, Gaestel M, Engel K & Buchner J (1993) Small heat shock proteins are molecular chaperones. J Biol Chem 268: 1517-1520.
    • (1993) J Biol Chem , vol.268 , pp. 1517-1520
    • Jakob, U.1    Gaestel, M.2    Engel, K.3    Buchner, J.4
  • 70
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob U, Lilie H, Meyer I & Buchner J (1995) Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J Biol Chem 270: 7288-7294.
    • (1995) J Biol Chem , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 71
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U, Muse W, Eser M & Bardwell JC (1999) Chaperone activity with a redox switch. Cell 96: 341-352.
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 72
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler KC, Waller PR & Sauer RT (1996) Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271: 990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 73
    • 0035011051 scopus 로고    scopus 로고
    • A connection between stress and development in the multicellular prokaryote Streptomyces coelicolor A3(2)
    • Kelemen GH, Viollier PH, Tenor J, Marri L, Buttner MJ & Thompson CJ (2001) A connection between stress and development in the multicellular prokaryote Streptomyces coelicolor A3(2). Mol Microbiol 40: 804-814.
    • (2001) Mol Microbiol , vol.40 , pp. 804-814
    • Kelemen, G.H.1    Viollier, P.H.2    Tenor, J.3    Marri, L.4    Buttner, M.J.5    Thompson, C.J.6
  • 74
    • 0342626726 scopus 로고    scopus 로고
    • Identification and transcriptional characterization of the gene encoding the stress-response sigma factor sigma(H) in streptomyces coelicolor A3(2)
    • Kormanec J, Sevcikova B, Halgasova N, Knirschova R & Rezuchova B (2000) Identification and transcriptional characterization of the gene encoding the stress-response sigma factor sigma(H) in streptomyces coelicolor A3(2). FEMS Microbiol Lett 189: 31-38.
    • (2000) FEMS Microbiol Lett , vol.189 , pp. 31-38
    • Kormanec, J.1    Sevcikova, B.2    Halgasova, N.3    Knirschova, R.4    Rezuchova, B.5
  • 76
    • 0142227208 scopus 로고    scopus 로고
    • The structure of ClpB: A molecular chaperone that rescues proteins from an aggregated state
    • Lee S, Sowa ME, Watanabe YH, Sigler PB, Chiu W, Yoshida M & Tsai FT (2003) The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state. Cell 115: 229-240.
    • (2003) Cell , vol.115 , pp. 229-240
    • Lee, S.1    Sowa, M.E.2    Watanabe, Y.H.3    Sigler, P.B.4    Chiu, W.5    Yoshida, M.6    Tsai, F.T.7
  • 77
    • 23844442155 scopus 로고    scopus 로고
    • A master regulator sigmaB governs osmotic and oxidative response as well as differentiation via a network of sigma factors in Streptomyces coelicolor
    • Lee EJ, Karoonuthaisiri N, Kim HS, Park JH, Cha CJ, Kao CM & Roe JH (2005) A master regulator sigmaB governs osmotic and oxidative response as well as differentiation via a network of sigma factors in Streptomyces coelicolor. Mol Microbiol 57: 1252-1264.
    • (2005) Mol Microbiol , vol.57 , pp. 1252-1264
    • Lee, E.J.1    Karoonuthaisiri, N.2    Kim, H.S.3    Park, J.H.4    Cha, C.J.5    Kao, C.M.6    Roe, J.H.7
  • 79
    • 1542373514 scopus 로고    scopus 로고
    • Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii
    • Leverrier P, Vissers JP, Rouault A, Boyaval P & Jan G (2004) Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii. Arch Microbiol 181: 215-230.
    • (2004) Arch Microbiol , vol.181 , pp. 215-230
    • Leverrier, P.1    Vissers, J.P.2    Rouault, A.3    Boyaval, P.4    Jan, G.5
  • 80
    • 0030070934 scopus 로고    scopus 로고
    • Crystallisation of the Bacillus subtilis sporulation inhibitor SinR, complexed with its antagonist, SinI
    • Lewis RJ, Brannigan JA, Smith I & Wilkinson AJ (1996) Crystallisation of the Bacillus subtilis sporulation inhibitor SinR, complexed with its antagonist, SinI. FEBS Lett 378: 98-100.
    • (1996) FEBS Lett , vol.378 , pp. 98-100
    • Lewis, R.J.1    Brannigan, J.A.2    Smith, I.3    Wilkinson, A.J.4
  • 82
    • 0033762339 scopus 로고    scopus 로고
    • Bifidobacterium strains from resident infant human gastrointestinal microflora exert antimicrobial activity
    • Lievin V, Peiffer I, Hudault S, Rochat F, Brassart D, Neeser JR & Servin AL (2000) Bifidobacterium strains from resident infant human gastrointestinal microflora exert antimicrobial activity. Gut 47: 646-652.
    • (2000) Gut , vol.47 , pp. 646-652
    • Lievin, V.1    Peiffer, I.2    Hudault, S.3    Rochat, F.4    Brassart, D.5    Neeser, J.R.6    Servin, A.L.7
  • 83
    • 0026612797 scopus 로고
    • The sigma 70 family: Sequence conservation and evolutionary relationships
    • Lonetto M, Gribskov M & Gross CA (1992) The sigma 70 family: sequence conservation and evolutionary relationships. J Bacteriol 174: 3843-3849.
    • (1992) J Bacteriol , vol.174 , pp. 3843-3849
    • Lonetto, M.1    Gribskov, M.2    Gross, C.A.3
  • 84
    • 0345580182 scopus 로고    scopus 로고
    • Conditional sigma factor expression, using the inducible acetamidase promoter, reveals that the Mycobacterium tuberculosis sigF gene modulates expression of the 16-kilodalton alpha-crystallin homologue
    • Manabe YC, Chen JM, Ko CG, Chen P & Bishai WR (1999) Conditional sigma factor expression, using the inducible acetamidase promoter, reveals that the Mycobacterium tuberculosis sigF gene modulates expression of the 16-kilodalton alpha-crystallin homologue. J Bacteriol 181: 7629-7633.
    • (1999) J Bacteriol , vol.181 , pp. 7629-7633
    • Manabe, Y.C.1    Chen, J.M.2    Ko, C.G.3    Chen, P.4    Bishai, W.R.5
  • 85
    • 0032955397 scopus 로고    scopus 로고
    • Differential expression of 10 sigma factor genes in Mycobacterium tuberculosis
    • Manganelli R, Dubnau E, Tyagi S, Kramer FR & Smith I (1999) Differential expression of 10 sigma factor genes in Mycobacterium tuberculosis. Mol Microbiol 31: 715-724.
    • (1999) Mol Microbiol , vol.31 , pp. 715-724
    • Manganelli, R.1    Dubnau, E.2    Tyagi, S.3    Kramer, F.R.4    Smith, I.5
  • 86
    • 0034903883 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis ECF sigma factor sigmaE: Role in global gene expression and survival in macrophages
    • Manganelli R, Voskuil MI, Schoolnik GK & Smith I (2001) The Mycobacterium tuberculosis ECF sigma factor sigmaE: role in global gene expression and survival in macrophages. Mol Microbiol 41: 423-437.
    • (2001) Mol Microbiol , vol.41 , pp. 423-437
    • Manganelli, R.1    Voskuil, M.I.2    Schoolnik, G.K.3    Smith, I.4
  • 87
    • 0036065206 scopus 로고    scopus 로고
    • Role of the extracytoplasmic-function sigma factor sigma(H) in Mycobacterium tuberculosis global gene expression
    • Manganelli R, Voskuil MI, Schoolnik GK, Dubnau E, Gomez M & Smith I (2002) Role of the extracytoplasmic-function sigma factor sigma(H) in Mycobacterium tuberculosis global gene expression. Mol Microbiol 45: 365-374.
    • (2002) Mol Microbiol , vol.45 , pp. 365-374
    • Manganelli, R.1    Voskuil, M.I.2    Schoolnik, G.K.3    Dubnau, E.4    Gomez, M.5    Smith, I.6
  • 89
    • 0025788262 scopus 로고
    • Characterization of the groEL-like genes in Streptomyces albus
    • Mazodier P, Guglielmi G, Davies J & Thompson CJ (1991) Characterization of the groEL-like genes in Streptomyces albus. J Bacteriol 173: 7382-7386.
    • (1991) J Bacteriol , vol.173 , pp. 7382-7386
    • Mazodier, P.1    Guglielmi, G.2    Davies, J.3    Thompson, C.J.4
  • 90
    • 0031745718 scopus 로고    scopus 로고
    • The extracytoplasmic function sigma factors: Role and regulation
    • Missiakas D & Raina S (1998) The extracytoplasmic function sigma factors: role and regulation. Mol Microbiol 28: 1059-1066.
    • (1998) Mol Microbiol , vol.28 , pp. 1059-1066
    • Missiakas, D.1    Raina, S.2
  • 91
    • 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 FX & 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
  • 92
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A, Tomoyasu T, Goloubinoff P, Rudiger S, Roder D, Langen H & Bukau B (1999) Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. Embo J 18: 6934-6949.
    • (1999) Embo J , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Roder, D.5    Langen, H.6    Bukau, B.7
  • 93
    • 3242690878 scopus 로고    scopus 로고
    • The genome sequence of the gram-positive sugarcane pathogen Leifsonia xyli subsp. xyli
    • Monteiro-Vitorello CB, Camargo LE, Van Sluys MA, et al. (2004) The genome sequence of the gram-positive sugarcane pathogen Leifsonia xyli subsp. xyli. Mol Plant Microbe Interact 17: 827-836.
    • (2004) Mol Plant Microbe Interact , vol.17 , pp. 827-836
    • Monteiro-Vitorello, C.B.1    Camargo, L.E.2    Van Sluys, M.A.3
  • 94
    • 0032944541 scopus 로고    scopus 로고
    • Negative regulation of bacterial heat shock genes
    • Narberhaus F (1999) Negative regulation of bacterial heat shock genes. Mol Microbiol 31: 1-8.
    • (1999) Mol Microbiol , vol.31 , pp. 1-8
    • Narberhaus, F.1
  • 95
    • 0036195722 scopus 로고    scopus 로고
    • Alpha-crystallin-type heat shock proteins: Socializing minichaperones in the context of a multichaperone network
    • table of contents
    • Narberhaus F (2002) Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol Mol Biol Rev 66: 64-93; table of contents.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 64-93
    • Narberhaus, F.1
  • 96
    • 2442452545 scopus 로고    scopus 로고
    • The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus
    • Newberry KJ & Brennan RG (2004) The structural mechanism for transcription activation by MerR family member multidrug transporter activation, N terminus. J Biol Chem 279: 20356-20362.
    • (2004) J Biol Chem , vol.279 , pp. 20356-20362
    • Newberry, K.J.1    Brennan, R.G.2
  • 98
    • 0038460070 scopus 로고    scopus 로고
    • Proteomic studies of diauxic lag in the differentiating prokaryote Streptomyces coelicolor reveal a regulatory network of stress-induced proteins and central metabolic enzymes
    • Novotna J, Vohradsky J, Berndt P, Gramajo H, Langen H, Li XM, Minas W, Orsaria L, Roeder D & Thompson CJ (2003) Proteomic studies of diauxic lag in the differentiating prokaryote Streptomyces coelicolor reveal a regulatory network of stress-induced proteins and central metabolic enzymes. Mol Microbiol 48: 1289-1303.
    • (2003) Mol Microbiol , vol.48 , pp. 1289-1303
    • Novotna, J.1    Vohradsky, J.2    Berndt, P.3    Gramajo, H.4    Langen, H.5    Li, X.M.6    Minas, W.7    Orsaria, L.8    Roeder, D.9    Thompson, C.J.10
  • 99
    • 0035834039 scopus 로고    scopus 로고
    • Genome sequence of an industrial microorganism Streptomyces avermitilis: Deducing the ability of producing secondary metabolites
    • Omura S, Ikeda H, Ishikawa J, et al. (2001) Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites. Proc Natl Acad Sci USA 98: 12215-12220.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 12215-12220
    • Omura, S.1    Ikeda, H.2    Ishikawa, J.3
  • 101
    • 0032898961 scopus 로고    scopus 로고
    • Evidence that the extracytoplasmic function sigma factor sigmaE is required for normal cell wall structure in Streptomyces coelicolor A3(2)
    • Paget MS, Chamberlin L, Atrih A, Foster SJ & Buttner MJ (1999) Evidence that the extracytoplasmic function sigma factor sigmaE is required for normal cell wall structure in Streptomyces coelicolor A3(2). J Bacteriol 181: 204-211.
    • (1999) J Bacteriol , vol.181 , pp. 204-211
    • Paget, M.S.1    Chamberlin, L.2    Atrih, A.3    Foster, S.J.4    Buttner, M.J.5
  • 102
    • 0030812638 scopus 로고    scopus 로고
    • The HtrA family of serine proteases
    • Pallen MJ & Wren BW (1997) The HtrA family of serine proteases. Mol Microbiol 26: 209-221.
    • (1997) Mol Microbiol , vol.26 , pp. 209-221
    • Pallen, M.J.1    Wren, B.W.2
  • 103
    • 0032541344 scopus 로고    scopus 로고
    • ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
    • Panaretou B, Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW & Pearl LH (1998) ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. Embo J 17: 4829-4836.
    • (1998) Embo J , vol.17 , pp. 4829-4836
    • Panaretou, B.1    Prodromou, C.2    Roe, S.M.3    O'Brien, R.4    Ladbury, J.E.5    Piper, P.W.6    Pearl, L.H.7
  • 104
    • 0029047507 scopus 로고
    • Developmental control of the heat-shock stress regulon in Streptomyces coelicolor
    • Puglia AM, Vohradsky J & Thompson CJ (1995) Developmental control of the heat-shock stress regulon in Streptomyces coelicolor. Mol Microbiol 17: 737-746.
    • (1995) Mol Microbiol , vol.17 , pp. 737-746
    • Puglia, A.M.1    Vohradsky, J.2    Thompson, C.J.3
  • 106
    • 0032035329 scopus 로고    scopus 로고
    • Positive activation of gene expression
    • Rhodius VA & Busby SJ (1998) Positive activation of gene expression. Curr Opin Microbiol 1: 152-159.
    • (1998) Curr Opin Microbiol , vol.1 , pp. 152-159
    • Rhodius, V.A.1    Busby, S.J.2
  • 107
    • 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 RC, Toochinda C, Avedissian M, Baldini RL, Gomes SL & Shapiro L (1996) Identification of a Caulobacter crescentus operon encoding hrcA, involved in negatively regulating heat-inducible transcription, and the chaperone gene grpE. J Bacteriol 178: 1829-1841.
    • (1996) J Bacteriol , 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
  • 108
    • 0032488632 scopus 로고    scopus 로고
    • The lon protease from Mycobacterium smegmatis: Molecular cloning, sequence analysis, functional expression, and enzymatic characterization
    • Roudiak SG, Seth A, Knipfer N & Shrader TE (1998) The lon protease from Mycobacterium smegmatis: molecular cloning, sequence analysis, functional expression, and enzymatic characterization. Biochemistry 37: 377-386.
    • (1998) Biochemistry , vol.37 , pp. 377-386
    • Roudiak, S.G.1    Seth, A.2    Knipfer, N.3    Shrader, T.E.4
  • 109
    • 21744455549 scopus 로고    scopus 로고
    • Effect of heat-shock and bile salts on protein synthesis of Bifidobacterium longum revealed by [35S]methionine labelling and two-dimensional gel electrophoresis
    • Savijoki K, Suokko A, Palva A, Valmu L, Kalkkinen N & Varmanen P (2005) Effect of heat-shock and bile salts on protein synthesis of Bifidobacterium longum revealed by [35S]methionine labelling and two-dimensional gel electrophoresis. FEMS Microbiol Lett 248: 207-215.
    • (2005) FEMS Microbiol Lett , vol.248 , pp. 207-215
    • Savijoki, K.1    Suokko, A.2    Palva, A.3    Valmu, L.4    Kalkkinen, N.5    Varmanen, P.6
  • 111
    • 14844336331 scopus 로고    scopus 로고
    • HspR is a global negative regulator of heat shock gene expression in Deinococcus radiodurans
    • Schmid AK, Howell HA, Battista JR, Peterson SN & Lidstrom ME (2005) HspR is a global negative regulator of heat shock gene expression in Deinococcus radiodurans. Mol Microbiol 55: 1579-1590.
    • (2005) Mol Microbiol , vol.55 , pp. 1579-1590
    • Schmid, A.K.1    Howell, H.A.2    Battista, J.R.3    Peterson, S.N.4    Lidstrom, M.E.5
  • 112
    • 0034630225 scopus 로고    scopus 로고
    • Basic features of the stress response in three species of bifidobacteria: B. longum, B. adolescentis, and B. breve
    • Schmidt G & Zink R (2000) Basic features of the stress response in three species of bifidobacteria: B. longum, B. adolescentis, and B. breve. Int J Food Microbiol 55: 41-45.
    • (2000) Int J Food Microbiol , vol.55 , pp. 41-45
    • Schmidt, G.1    Zink, R.2
  • 113
    • 0029984172 scopus 로고    scopus 로고
    • Regulation and organization of the groE and dnaK operons in Eubacteria
    • Segal R & Ron EZ (1996) Regulation and organization of the groE and dnaK operons in Eubacteria. FEMS Microbiol Lett 138: 1-10.
    • (1996) FEMS Microbiol Lett , vol.138 , pp. 1-10
    • Segal, R.1    Ron, E.Z.2
  • 114
    • 0029074488 scopus 로고
    • Characterization of Streptomyces albus 18-kilodalton heat shock-responsive protein
    • Servant P & Mazodier P (1995) Characterization of Streptomyces albus 18-kilodalton heat shock-responsive protein. J Bacteriol 177: 2998-3003.
    • (1995) J Bacteriol , vol.177 , pp. 2998-3003
    • Servant, P.1    Mazodier, P.2
  • 115
    • 0030465351 scopus 로고    scopus 로고
    • Heat induction of hsp18 gene expression in Streptomyces albus G: Transcriptional and posttranscriptional regulation
    • Servant P & Mazodier P (1996) Heat induction of hsp18 gene expression in Streptomyces albus G: transcriptional and posttranscriptional regulation. J Bacteriol 178: 7031-7036.
    • (1996) J Bacteriol , vol.178 , pp. 7031-7036
    • Servant, P.1    Mazodier, P.2
  • 116
    • 0035731116 scopus 로고    scopus 로고
    • Negative regulation of the heat shock response in Streptomyces
    • Servant P & Mazodier P (2001) Negative regulation of the heat shock response in Streptomyces. Arch Microbiol 176: 237-242.
    • (2001) Arch Microbiol , vol.176 , pp. 237-242
    • Servant, P.1    Mazodier, P.2
  • 117
    • 0032846818 scopus 로고    scopus 로고
    • RheA, the repressor of hsp18 in Streptomyces albus G
    • Servant P, Rapoport G & Mazodier P (1999) RheA, the repressor of hsp18 in Streptomyces albus G. Microbiology 145: 2385-2391.
    • (1999) Microbiology , vol.145 , pp. 2385-2391
    • Servant, P.1    Rapoport, G.2    Mazodier, P.3
  • 118
    • 0034724328 scopus 로고    scopus 로고
    • The RheA repressor is the thermosensor of the HSP18 heat shock response in Streptomyces albus
    • Servant P, Grandvalet C & Mazodier P (2000) The RheA repressor is the thermosensor of the HSP18 heat shock response in Streptomyces albus. Proc Natl Acad Sci USA 97: 3538-3543.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3538-3543
    • Servant, P.1    Grandvalet, C.2    Mazodier, P.3
  • 119
    • 20444484956 scopus 로고    scopus 로고
    • Intrinsic tolerance of Bifidobacterium species to heat and oxygen and survival following spray drying and storage
    • Simpson PJ, Stanton C, Fitzgerald GF & Ross RP (2005) Intrinsic tolerance of Bifidobacterium species to heat and oxygen and survival following spray drying and storage. J Appl Microbiol 99: 493-501.
    • (2005) J Appl Microbiol , vol.99 , pp. 493-501
    • Simpson, P.J.1    Stanton, C.2    Fitzgerald, G.F.3    Ross, R.P.4
  • 120
    • 0035986649 scopus 로고    scopus 로고
    • The lon gene, encoding an ATP-dependent protease, is a novel member of the HAIR/HspR stress-response regulon in actinomycetes
    • Sobczyk A, Bellier A, Viala J & Mazodier P (2002) The lon gene, encoding an ATP-dependent protease, is a novel member of the HAIR/HspR stress-response regulon in actinomycetes. Microbiology 148: 1931-1937.
    • (2002) Microbiology , vol.148 , pp. 1931-1937
    • Sobczyk, A.1    Bellier, A.2    Viala, J.3    Mazodier, P.4
  • 122
    • 0242521392 scopus 로고    scopus 로고
    • RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH
    • Song T, Dove SL, Lee KH & Husson RN (2003) RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH. Mol Microbiol 50: 949-959.
    • (2003) Mol Microbiol , vol.50 , pp. 949-959
    • Song, T.1    Dove, S.L.2    Lee, K.H.3    Husson, R.N.4
  • 123
    • 0032730207 scopus 로고    scopus 로고
    • The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori
    • Spohn G & Scarlato V (1999) The autoregulatory HspR repressor protein governs chaperone gene transcription in Helicobacter pylori. Mol Microbiol 34: 663-674.
    • (1999) Mol Microbiol , vol.34 , pp. 663-674
    • Spohn, G.1    Scarlato, V.2
  • 124
    • 3042818394 scopus 로고    scopus 로고
    • Heat-shock proteins and the host-pathogen interaction during bacterial infection
    • Stewart GR & Young DB (2004) Heat-shock proteins and the host-pathogen interaction during bacterial infection. Curr Opin Immunol 16: 506-510.
    • (2004) Curr Opin Immunol , vol.16 , pp. 506-510
    • Stewart, G.R.1    Young, D.B.2
  • 131
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: Comparison with ClpA, ClpB, and HtpG in vivo
    • Thomas JG & Baneyx F (1998) Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG in vivo. J Bacteriol 180: 5165-5172.
    • (1998) J Bacteriol , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 133
    • 8144219531 scopus 로고    scopus 로고
    • Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003: Genetic, transcriptional, and phylogenetic analyses
    • Ventura M, Canchaya C, Zink R, Fitzgerald GF & van Sinderen D (2004a) Characterization of the groEL and groES loci in Bifidobacterium breve UCC 2003: genetic, transcriptional, and phylogenetic analyses. Appl Environ Microbiol 70: 6197-6209.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 6197-6209
    • Ventura, M.1    Canchaya, C.2    Zink, R.3    Fitzgerald, G.F.4    Van Sinderen, D.5
  • 135
    • 24944502086 scopus 로고    scopus 로고
    • Genetic and transcriptional organization of the clpC locus in Bifidobacterium breve UCC 2003
    • Ventura M, Fitzgerald GF & Van Sinderen D (2005a) Genetic and transcriptional organization of the clpC locus in Bifidobacterium breve UCC 2003. Appl Environ Microbiol 71: 6282-6291.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 6282-6291
    • Ventura, M.1    Fitzgerald, G.F.2    Van Sinderen, D.3
  • 136
    • 24944547568 scopus 로고    scopus 로고
    • The clpB gene of Bifidobacterium breve UCC 2003: Transcriptional analysis and first insights into stress induction
    • Ventura M, Kenny JG, Zhang Z, Fitzgerald GF & van Sinderen D (2005b) The clpB gene of Bifidobacterium breve UCC 2003: transcriptional analysis and first insights into stress induction. Microbiology 151: 2861-2872.
    • (2005) Microbiology , vol.151 , pp. 2861-2872
    • Ventura, M.1    Kenny, J.G.2    Zhang, Z.3    Fitzgerald, G.F.4    Van Sinderen, D.5
  • 137
    • 12244311206 scopus 로고    scopus 로고
    • Gene structure and transcriptional organization of the dnaK operon of Bifidobacterium breve UCC 2003 and application of the operon in bifidobacterial tracing
    • Ventura M, Zink R, Fitzgerald GF & van Sinderen D (2005c) Gene structure and transcriptional organization of the dnaK operon of Bifidobacterium breve UCC 2003 and application of the operon in bifidobacterial tracing. Appl Environ Microbiol 71: 487-500.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 487-500
    • Ventura, M.1    Zink, R.2    Fitzgerald, G.F.3    Van Sinderen, D.4
  • 140
    • 0033678713 scopus 로고    scopus 로고
    • The clpP multigenic family in Streptomyces lividans: Conditional expression of the clpP3 clpP4 operon is controlled by PopR, a novel transcriptional activator
    • Viala J, Rapoport G & Mazodier P (2000) The clpP multigenic family in Streptomyces lividans: conditional expression of the clpP3 clpP4 operon is controlled by PopR, a novel transcriptional activator. Mol Microbiol 38: 602-612.
    • (2000) Mol Microbiol , vol.38 , pp. 602-612
    • Viala, J.1    Rapoport, G.2    Mazodier, P.3
  • 141
    • 0030817690 scopus 로고    scopus 로고
    • Identification of procaryotic developmental stages by statistical analyses of two-dimensional gel patterns
    • Vohradsky J, Li XM & Thompson CJ (1997) Identification of procaryotic developmental stages by statistical analyses of two-dimensional gel patterns. Electrophoresis 18: 1418-1428.
    • (1997) Electrophoresis , vol.18 , pp. 1418-1428
    • Vohradsky, J.1    Li, X.M.2    Thompson, C.J.3
  • 142
    • 0033895843 scopus 로고    scopus 로고
    • Developmental control of stress stimulons in Streptomyces coelicolor revealed by statistical analyses of global gene expression patterns
    • Vohradsky J, Li XM, Dale G, Folcher M, Nguyen L, Viollier PH & Thompson CJ (2000) Developmental control of stress stimulons in Streptomyces coelicolor revealed by statistical analyses of global gene expression patterns. J Bacteriol 182: 4979-4986.
    • (2000) J Bacteriol , vol.182 , pp. 4979-4986
    • Vohradsky, J.1    Li, X.M.2    Dale, G.3    Folcher, M.4    Nguyen, L.5    Viollier, P.H.6    Thompson, C.J.7
  • 143
    • 0030691115 scopus 로고    scopus 로고
    • The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
    • Wang J, Hartling JA & Flanagan JM (1997) The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis. Cell 91: 447-456.
    • (1997) Cell , vol.91 , pp. 447-456
    • Wang, J.1    Hartling, J.A.2    Flanagan, J.M.3
  • 144
    • 0033520987 scopus 로고    scopus 로고
    • Posttranslational quality control: Folding, refolding, and degrading proteins
    • Wickner S, Maurizi MR & Gottesman S (1999) Posttranslational quality control: folding, refolding, and degrading proteins. Science 286: 1888-1893.
    • (1999) Science , vol.286 , pp. 1888-1893
    • Wickner, S.1    Maurizi, M.R.2    Gottesman, S.3
  • 145
    • 0030595337 scopus 로고    scopus 로고
    • Structural classification of HTH DNA-binding domains and protein-DNA interaction modes
    • Wintjens R & Rooman M(1996) Structural classification of HTH DNA-binding domains and protein-DNA interaction modes. J Mol Biol 262: 294-313.
    • (1996) J Mol Biol , vol.262 , pp. 294-313
    • Wintjens, R.1    Rooman, M.2
  • 146
    • 0031973901 scopus 로고    scopus 로고
    • The CspA family in Escherichia coli: Multiple gene duplication for stress adaptation
    • Yamanaka K, Fang L & Inouye M (1998) The CspA family in Escherichia coli: multiple gene duplication for stress adaptation. Mol Microbiol 27: 247-255.
    • (1998) Mol Microbiol , vol.27 , pp. 247-255
    • Yamanaka, K.1    Fang, L.2    Inouye, M.3
  • 147
    • 0029560312 scopus 로고
    • Regulation of groE expression in Bacillus subtilis: The involvement of the sigma A-like promoter and the roles of the inverted repeat sequence (CIRCE)
    • Yuan G & Wong SL (1995) Regulation of groE expression in Bacillus subtilis: the involvement of the sigma A-like promoter and the roles of the inverted repeat sequence (CIRCE). J Bacteriol 177: 5427-5433.
    • (1995) J Bacteriol , vol.177 , pp. 5427-5433
    • Yuan, G.1    Wong, S.L.2
  • 148
    • 0033118799 scopus 로고    scopus 로고
    • Regulation of the heat-shock response
    • Yura T & Nakahigashi K (1999) Regulation of the heat-shock response. Curr Opin Microbiol 2: 153-158.
    • (1999) Curr Opin Microbiol , vol.2 , pp. 153-158
    • Yura, T.1    Nakahigashi, K.2
  • 149
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura T, Nagai H & 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
  • 150
    • 0027521148 scopus 로고
    • Heat induction of sigma 32 synthesis mediated by mRNA secondary structure: A primary step of the heat shock response in Escherichia coli
    • Yuzawa H, Nagai H, Mori H & Yura T (1993) Heat induction of sigma 32 synthesis mediated by mRNA secondary structure: a primary step of the heat shock response in Escherichia coli. Nucleic Acids Res 21: 5449-5455.
    • (1993) Nucleic Acids Res , vol.21 , pp. 5449-5455
    • Yuzawa, H.1    Nagai, H.2    Mori, H.3    Yura, T.4
  • 151
    • 0028292919 scopus 로고
    • CIRCE, a novel heat shock element involved in regulation of heat shock operon dnaK of Bacillus subtilis
    • Zuber U & 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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