메뉴 건너뛰기




Volumn 106, Issue 4, 2008, Pages 324-336

Molecular Chaperones in Lactic Acid Bacteria: Physiological Consequences and Biochemical Properties

Author keywords

lactic acid bacteria; molecular chaperone; stress response

Indexed keywords

ACIDS; APPLICATIONS; BACTERIOLOGY; BIOCHEMICAL ENGINEERING; BODY FLUIDS; DAIRY PRODUCTS; ELASTICITY; INDUSTRIAL APPLICATIONS; LABORATORIES; LACTIC ACID; ORGANIC ACIDS;

EID: 55549143027     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1263/jbb.106.324     Document Type: Article
Times cited : (52)

References (130)
  • 2
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl F.U. Molecular chaperones in cellular protein folding. Nature 381 (1996) 571-580
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 4
    • 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 J.G., and Baneyx F. 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 (1998) 5165-5172
    • (1998) J. Bacteriol. , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 7
    • 13244279524 scopus 로고    scopus 로고
    • Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33
    • Winter J., Linke K., Jatzek A., and Jakob U. Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33. Mol. Cell 17 (2005) 381-392
    • (2005) Mol. Cell , vol.17 , pp. 381-392
    • Winter, J.1    Linke, K.2    Jatzek, A.3    Jakob, U.4
  • 8
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • Jakob U., Muse W., Eser M., and Bardwell J.C. Chaperone activity with a redox switch. Cell 96 (1999) 341-352
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.4
  • 9
    • 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. The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J. Bacteriol. 171 (1989) 1379-1385
    • (1989) J. Bacteriol. , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 10
    • 33646907087 scopus 로고    scopus 로고
    • GroEL-GroES-mediated protein folding
    • Horwich A.L., Farr G.W., and Fenton W.A. GroEL-GroES-mediated protein folding. Chem Rev. 106 (2006) 1917-1930
    • (2006) Chem Rev. , vol.106 , pp. 1917-1930
    • Horwich, A.L.1    Farr, G.W.2    Fenton, W.A.3
  • 12
    • 35748962910 scopus 로고    scopus 로고
    • The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions
    • Genevaux P., Georgopoulos C., and Kelley W.L. The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol. Microbiol. 66 (2007) 840-857
    • (2007) Mol. Microbiol. , vol.66 , pp. 840-857
    • Genevaux, P.1    Georgopoulos, C.2    Kelley, W.L.3
  • 13
    • 0024421347 scopus 로고
    • Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures
    • Bukau B., and Walker G.C. Delta dnaK52 mutants of Escherichia coli have defects in chromosome segregation and plasmid maintenance at normal growth temperatures. J. Bacteriol. 171 (1989) 6030-6038
    • (1989) J. Bacteriol. , vol.171 , pp. 6030-6038
    • Bukau, B.1    Walker, G.C.2
  • 14
    • 0024672180 scopus 로고
    • Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism
    • Bukau B., and Walker G.C. Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism. J. Bacteriol. 171 (1989) 2337-2346
    • (1989) J. Bacteriol. , vol.171 , pp. 2337-2346
    • Bukau, B.1    Walker, G.C.2
  • 15
    • 0025048776 scopus 로고
    • Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone
    • Bukau B., and Walker G.C. Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone. EMBO J. 9 (1990) 4027-4036
    • (1990) EMBO J. , vol.9 , pp. 4027-4036
    • Bukau, B.1    Walker, G.C.2
  • 16
    • 0025769565 scopus 로고
    • Role of heat shock protein DnaK in osmotic adaptation of Escherichia coli
    • Meury J., and Kohiyama M. Role of heat shock protein DnaK in osmotic adaptation of Escherichia coli. J. Bacteriol. 173 (1991) 4404-4410
    • (1991) J. Bacteriol. , vol.173 , pp. 4404-4410
    • Meury, J.1    Kohiyama, M.2
  • 17
    • 0026707466 scopus 로고
    • DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli
    • Shi W., Zhou Y., Wild J., Adler J., and Gross C.A. DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli. J. Bacteriol. 174 (1992) 6256-6263
    • (1992) J. Bacteriol. , vol.174 , pp. 6256-6263
    • Shi, W.1    Zhou, Y.2    Wild, J.3    Adler, J.4    Gross, C.A.5
  • 19
    • 0032557562 scopus 로고    scopus 로고
    • Involvement of molecular chaperonins in nucleotide excision repair. DnaK leads to increased thermal stability of UvrA, catalytic UvrB loading, enhanced repair, and increased UV resistance
    • Zou Y., Crowley D.J., and Van Houten B. Involvement of molecular chaperonins in nucleotide excision repair. DnaK leads to increased thermal stability of UvrA, catalytic UvrB loading, enhanced repair, and increased UV resistance. J. Biol. Chem. 273 (1998) 12887-12892
    • (1998) J. Biol. Chem. , vol.273 , pp. 12887-12892
    • Zou, Y.1    Crowley, D.J.2    Van Houten, B.3
  • 20
    • 0034911990 scopus 로고    scopus 로고
    • Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins
    • Tokumoto U., and Takahashi Y. Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. J. Biochem. 130 (2001) 63-71
    • (2001) J. Biochem. , vol.130 , pp. 63-71
    • Tokumoto, U.1    Takahashi, Y.2
  • 21
    • 0032541496 scopus 로고    scopus 로고
    • Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli
    • Hesterkamp T., and Bukau B. Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J. 17 (1998) 4818-4828
    • (1998) EMBO J. , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 22
    • 0035910560 scopus 로고    scopus 로고
    • The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli
    • Silberg J.J., Hoff K.G., Tapley T.L., and Vickery L.E. The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 276 (2001) 1696-1700
    • (2001) J. Biol. Chem. , vol.276 , pp. 1696-1700
    • Silberg, J.J.1    Hoff, K.G.2    Tapley, T.L.3    Vickery, L.E.4
  • 24
    • 0037174883 scopus 로고    scopus 로고
    • Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones
    • Kluck C.J., Patzelt H., Genevaux P., Brehmer D., Rist W., Schneider-Mergener J., Bukau B., and Mayer M.P. Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones. J. Biol. Chem. 277 (2002) 41060-41069
    • (2002) J. Biol. Chem. , vol.277 , pp. 41060-41069
    • Kluck, C.J.1    Patzelt, H.2    Genevaux, P.3    Brehmer, D.4    Rist, W.5    Schneider-Mergener, J.6    Bukau, B.7    Mayer, M.P.8
  • 25
    • 0036810483 scopus 로고    scopus 로고
    • Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question
    • Dougan D.A., Mogk A., and Bukau B. Protein folding and degradation in bacteria: to degrade or not to degrade? That is the question. Cell. Mol. Life Sci. 59 (2002) 1607-1616
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1607-1616
    • Dougan, D.A.1    Mogk, A.2    Bukau, B.3
  • 26
    • 0023752052 scopus 로고
    • The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component
    • Katayama Y., Gottesman S., Pumphrey J., Rudikoff S., Clark W.P., and Maurizi M.R. The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component. J. Biol. Chem. 263 (1988) 15226-15236
    • (1988) J. Biol. Chem. , vol.263 , pp. 15226-15236
    • Katayama, Y.1    Gottesman, S.2    Pumphrey, J.3    Rudikoff, S.4    Clark, W.P.5    Maurizi, M.R.6
  • 27
    • 0025799542 scopus 로고
    • ClpB is the Escherichia coli heat shock protein F84.1
    • Squires C.L., Pedersen S., Ross B.M., and Squires C. ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173 (1991) 4254-4262
    • (1991) J. Bacteriol. , vol.173 , pp. 4254-4262
    • Squires, C.L.1    Pedersen, S.2    Ross, B.M.3    Squires, C.4
  • 28
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P., Mogk A., Zvi A.P., Tomoyasu T., and Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. USA 96 (1999) 13732-13737
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 29
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli
    • Zolkiewski M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J. Biol. Chem. 274 (1999) 28083-28086
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1
  • 30
    • 0027364289 scopus 로고
    • ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities
    • Gottesman S., Clark W.P., de Crecy-Lagard V., and Maurizi M.R. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities. J. Biol. Chem. 268 (1993) 22618-22626
    • (1993) J. Biol. Chem. , vol.268 , pp. 22618-22626
    • Gottesman, S.1    Clark, W.P.2    de Crecy-Lagard, V.3    Maurizi, M.R.4
  • 31
    • 0030569512 scopus 로고    scopus 로고
    • Disruption of the hslU gene, which encodes an ATPase subunit of the eukaryotic 26S proteasome homolog in Escherichia coli, suppresses the temperature-sensitive dnaA46 mutation
    • Katayama T., Kubota T., Takata M., Akimitsu N., and Sekimizu K. Disruption of the hslU gene, which encodes an ATPase subunit of the eukaryotic 26S proteasome homolog in Escherichia coli, suppresses the temperature-sensitive dnaA46 mutation. Biochem. Biophys. Res. Commun. 229 (1996) 219-224
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 219-224
    • Katayama, T.1    Kubota, T.2    Takata, M.3    Akimitsu, N.4    Sekimizu, K.5
  • 32
    • 0030462757 scopus 로고    scopus 로고
    • Identification and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli
    • Missiakas D., Schwager F., Betton J.M., Georgopoulos C., and Raina S. Identification and characterization of HslV HslU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli. EMBO J. 15 (1996) 6899-6909
    • (1996) EMBO J. , vol.15 , pp. 6899-6909
    • Missiakas, D.1    Schwager, F.2    Betton, J.M.3    Georgopoulos, C.4    Raina, S.5
  • 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., and Bukau B. Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 400 (1999) 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
    • 0034708485 scopus 로고    scopus 로고
    • A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding
    • Minami Y., Kawasaki H., Minami M., Tanahashi N., Tanaka K., and Yahara I. A critical role for the proteasome activator PA28 in the Hsp90-dependent protein refolding. J. Biol. Chem. 275 (2000) 9055-9061
    • (2000) J. Biol. Chem. , vol.275 , pp. 9055-9061
    • Minami, Y.1    Kawasaki, H.2    Minami, M.3    Tanahashi, N.4    Tanaka, K.5    Yahara, I.6
  • 36
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder H., Langer T., Hartl F.U., and Bukau B. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12 (1993) 4137-4144
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.U.3    Bukau, B.4
  • 37
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B., and Horwich A.L. The Hsp70 and Hsp60 chaperone machines. Cell 92 (1998) 351-366
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 39
    • 0029978528 scopus 로고    scopus 로고
    • Relationship between stress responses toward bile salts, acid and heat treatment in Enterococcus faecalis
    • Flahaunt S., Hartke A., Giard J.C., Benachour A., Boutibonnes P., and Auffray Y. Relationship between stress responses toward bile salts, acid and heat treatment in Enterococcus faecalis. FEMS Microbiol. Lett. 138 (1996) 49-54
    • (1996) FEMS Microbiol. Lett. , vol.138 , pp. 49-54
    • Flahaunt, S.1    Hartke, A.2    Giard, J.C.3    Benachour, A.4    Boutibonnes, P.5    Auffray, Y.6
  • 40
    • 0030895818 scopus 로고    scopus 로고
    • Induction of heat shock proteins DnaK, GroEL, and GroES by salt stress in Lactococcus lactis
    • Kilstrup M., Jacobsen S., Hammer K., and Vogensen F.K. Induction of heat shock proteins DnaK, GroEL, and GroES by salt stress in Lactococcus lactis. Appl. Environ. Microbiol. 63 (1997) 1826-1837
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1826-1837
    • Kilstrup, M.1    Jacobsen, S.2    Hammer, K.3    Vogensen, F.K.4
  • 41
    • 0029096159 scopus 로고
    • Expression of DnaK and GroEL homologs in Leuconstoc mesenteroides in response to heat shock, cold shock or chemical stress
    • Salotra P., Singh D.K., Seal K.P., Krishna N., Jaffe H., and Bhatnagar R. Expression of DnaK and GroEL homologs in Leuconstoc mesenteroides in response to heat shock, cold shock or chemical stress. FEMS Microbiol. Lett. 131 (1995) 57-62
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 57-62
    • Salotra, P.1    Singh, D.K.2    Seal, K.P.3    Krishna, N.4    Jaffe, H.5    Bhatnagar, R.6
  • 42
    • 0037901299 scopus 로고    scopus 로고
    • Multiple stress response in Streptococcus mutans and the induction of general and stress-specific proteins
    • Svensater G., Sjogreen B., and Hamilton I.R. Multiple stress response in Streptococcus mutans and the induction of general and stress-specific proteins. Microbiology 146 (2000) 107-117
    • (2000) Microbiology , vol.146 , pp. 107-117
    • Svensater, G.1    Sjogreen, B.2    Hamilton, I.R.3
  • 45
    • 33846942977 scopus 로고    scopus 로고
    • Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria
    • Frees D., Savijoki K., Varmanen P., and Ingmer H. Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria. Mol. Microbiol. 63 (2007) 1285-1295
    • (2007) Mol. Microbiol. , vol.63 , pp. 1285-1295
    • Frees, D.1    Savijoki, K.2    Varmanen, P.3    Ingmer, H.4
  • 46
    • 0030034307 scopus 로고    scopus 로고
    • Heat-shock and general stress response in Bacillus subtilis
    • Hecker M., Schumann W., and Volker U. Heat-shock and general stress response in Bacillus subtilis. Mol. Microbiol. 19 (1996) 417-428
    • (1996) Mol. Microbiol. , vol.19 , pp. 417-428
    • Hecker, M.1    Schumann, W.2    Volker, U.3
  • 47
    • 0032944541 scopus 로고    scopus 로고
    • Negative regulation of bacterial heat shock genes
    • Narberhaus F. Negative regulation of bacterial heat shock genes. Mol. Microbiol. 31 (1999) 1-8
    • (1999) Mol. Microbiol. , vol.31 , pp. 1-8
    • Narberhaus, F.1
  • 48
    • 0031876826 scopus 로고    scopus 로고
    • Induced levels of heat shock proteins in a dnaK mutant of Lactococcus lactis
    • Koch B., Kilstrup M., Vogensen F.K., and Hammer K. Induced levels of heat shock proteins in a dnaK mutant of Lactococcus lactis. J. Bacteriol. 180 (1998) 3873-3881
    • (1998) J. Bacteriol. , vol.180 , pp. 3873-3881
    • Koch, B.1    Kilstrup, M.2    Vogensen, F.K.3    Hammer, K.4
  • 49
    • 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. The GroE chaperonin machine is a major modulator of the CIRCE heat shock regulon of Bacillus subtilis. EMBO J. 16 (1997) 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
  • 51
    • 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
    • Derré I., Rapoport G., and Msadek T. CtsR, a novel regulator of stress and heat shock response, controls clp and molecular chaperone gene expression in Gram-positive bacteria. Mol. Microbiol. 31 (1999) 117-131
    • (1999) Mol. Microbiol. , vol.31 , pp. 117-131
    • Derré, I.1    Rapoport, G.2    Msadek, T.3
  • 52
    • 0037224322 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis heat shock gene htpG is under positive control
    • Versteeg S., Escher A., Wende A., Wiegert T., and Schumann W. Regulation of the Bacillus subtilis heat shock gene htpG is under positive control. J. Bacteriol. 185 (2003) 466-474
    • (2003) J. Bacteriol. , vol.185 , pp. 466-474
    • Versteeg, S.1    Escher, A.2    Wende, A.3    Wiegert, T.4    Schumann, W.5
  • 53
    • 33746675641 scopus 로고    scopus 로고
    • The CssRS two-component regulatory system controls a general secretion stress response in Bacillus subtilis.
    • Westers H., Westers L., Darmon E., van Dijl J.M., Quax W.J., and Zanen G. The CssRS two-component regulatory system controls a general secretion stress response in Bacillus subtilis. FEBS J. 273 (2006) 3816-3827
    • (2006) FEBS J. , vol.273 , pp. 3816-3827
    • Westers, H.1    Westers, L.2    Darmon, E.3    van Dijl, J.M.4    Quax, W.J.5    Zanen, G.6
  • 55
    • 0034319185 scopus 로고    scopus 로고
    • Molecular biology of oxygen tolerance in lactic acid bacteria: functions of NADH oxidases and Dpr in oxidative stress
    • Higuchi M., Yamamoto Y., and Kamio Y. Molecular biology of oxygen tolerance in lactic acid bacteria: functions of NADH oxidases and Dpr in oxidative stress. J. Biosci. Bioeng. 5 (2000) 484-493
    • (2000) J. Biosci. Bioeng. , vol.5 , pp. 484-493
    • Higuchi, M.1    Yamamoto, Y.2    Kamio, Y.3
  • 56
    • 33846945050 scopus 로고    scopus 로고
    • The small heat shock proteins and their clients
    • Nakamoto H., and Vígh L. The small heat shock proteins and their clients. Cell. Mol. Life Sci. 64 (2007) 294-306
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 294-306
    • Nakamoto, H.1    Vígh, L.2
  • 57
    • 21744436278 scopus 로고    scopus 로고
    • The activation mechanism of Hsp26 does not require dissociation of the oligomer
    • Franzmann T.M., Wühr M., Richter K., Walter S., and Buchner J. The activation mechanism of Hsp26 does not require dissociation of the oligomer. J. Mol. Biol. 350 (2005) 1083-1093
    • (2005) J. Mol. Biol. , vol.350 , pp. 1083-1093
    • Franzmann, T.M.1    Wühr, M.2    Richter, K.3    Walter, S.4    Buchner, J.5
  • 58
    • 29144527460 scopus 로고    scopus 로고
    • Small heat shock proteins: molecular structure and chaperone function
    • Sun Y., and MacRae T.H. Small heat shock proteins: molecular structure and chaperone function. Cell. Mol. Life Sci. 62 (2005) 2460-2476
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2460-2476
    • Sun, Y.1    MacRae, T.H.2
  • 59
    • 1542320089 scopus 로고    scopus 로고
    • The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions
    • Basha E., Lee G.J., Breci L.A., Hausrath A.C., Buan N.R., Giese K.C., and Vierling E. The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions. J. Biol. Chem. 279 (2004) 7566-7575
    • (2004) J. Biol. Chem. , vol.279 , pp. 7566-7575
    • Basha, E.1    Lee, G.J.2    Breci, L.A.3    Hausrath, A.C.4    Buan, N.R.5    Giese, K.C.6    Vierling, E.7
  • 60
    • 0032729809 scopus 로고    scopus 로고
    • The Oenococcus oeni clpX homologue is a heat shock gene preferentially expressed in exponential growth phase
    • Jobin M.P., Garmyn D., Diviès C., and Guzzo J. The Oenococcus oeni clpX homologue is a heat shock gene preferentially expressed in exponential growth phase. J. Bacteriol. 181 (1999) 6634-6641
    • (1999) J. Bacteriol. , vol.181 , pp. 6634-6641
    • Jobin, M.P.1    Garmyn, D.2    Diviès, C.3    Guzzo, J.4
  • 61
    • 32044462709 scopus 로고    scopus 로고
    • A small Hsp, Lo18, interacts with the cell membrane and modulates lipid physical state under heat shock conditions in a lactic acid bacterium
    • Coucheney F., Gal L., Beney L., Lherminier J., Gervais P., and Guzzo J. A small Hsp, Lo18, interacts with the cell membrane and modulates lipid physical state under heat shock conditions in a lactic acid bacterium. Biochim. Biophys. Acta 1720 (2005) 92-98
    • (2005) Biochim. Biophys. Acta , vol.1720 , pp. 92-98
    • Coucheney, F.1    Gal, L.2    Beney, L.3    Lherminier, J.4    Gervais, P.5    Guzzo, J.6
  • 62
    • 0034859278 scopus 로고    scopus 로고
    • Biochemical and physiological studies of the small heat shock protein Lo18 from the lactic acid bacterium Oenococcus oeni
    • Delmas F., Pierre F., Coucheney F., Divies C., and Guzzo J. Biochemical and physiological studies of the small heat shock protein Lo18 from the lactic acid bacterium Oenococcus oeni. J. Mol. Microbiol. Biotechnol. 3 (2001) 601-610
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 601-610
    • Delmas, F.1    Pierre, F.2    Coucheney, F.3    Divies, C.4    Guzzo, J.5
  • 63
    • 0042530403 scopus 로고    scopus 로고
    • Application of the shsp gene, encoding a small heat shock protein, as a food-grade selection marker for lactic acid bacteria
    • Demerdash H.A., Heller K.J., and Geis A. Application of the shsp gene, encoding a small heat shock protein, as a food-grade selection marker for lactic acid bacteria. Appl. Environ. Microbiol. 69 (2003) 4408-4412
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4408-4412
    • Demerdash, H.A.1    Heller, K.J.2    Geis, A.3
  • 64
    • 36348946895 scopus 로고    scopus 로고
    • Improved adaptation to heat, cold, and solvent tolerance in Lactobacillus plantarum
    • Fiocco D., Capozzi V., Goffin P., Hols P., and Spano G. Improved adaptation to heat, cold, and solvent tolerance in Lactobacillus plantarum. Appl. Microbiol. Biotechnol. 77 (2007) 909-915
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 909-915
    • Fiocco, D.1    Capozzi, V.2    Goffin, P.3    Hols, P.4    Spano, G.5
  • 65
    • 0030942271 scopus 로고    scopus 로고
    • Molecular characterization of the gene encoding an 18-kilodalton small heat shock protein associated with the membrane of Leuconostoc oenos
    • Jobin M.P., Delmas F., Garmyn D., Diviès C., and Guzzo J. Molecular characterization of the gene encoding an 18-kilodalton small heat shock protein associated with the membrane of Leuconostoc oenos. Appl. Environ. Microbiol. 63 (1997) 609-614
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 609-614
    • Jobin, M.P.1    Delmas, F.2    Garmyn, D.3    Diviès, C.4    Guzzo, J.5
  • 66
    • 34547190128 scopus 로고    scopus 로고
    • Molecular characterization of hsp20, encoding a small heat shock protein of Bifidobacterium breve UCC2003
    • Ventura M., Canchaya C., Zhang Z., Fitzgerald G.F., and van Sinderen D. Molecular characterization of hsp20, encoding a small heat shock protein of Bifidobacterium breve UCC2003. Appl. Environ. Microbiol. 73 (2007) 4695-4703
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 4695-4703
    • Ventura, M.1    Canchaya, C.2    Zhang, Z.3    Fitzgerald, G.F.4    van Sinderen, D.5
  • 67
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein
    • Flaherty M.K., DeLuca-Flaherty C., McKay B.D., and Mckay D.B. Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein. Nature 346 (1990) 623-628
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, M.K.1    DeLuca-Flaherty, C.2    McKay, B.D.3    Mckay, D.B.4
  • 68
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison C.J., Hayer-Hartl M., Liberto M.D., Hartl F.U., and Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276 (1997) 431-435
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Liberto, M.D.3    Hartl, F.U.4    Kuriyan, J.5
  • 71
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • Jiang J., Prasad K., Lafer E.M., and Sousa R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol. Cell 20 (2005) 513-524
    • (2005) Mol. Cell , vol.20 , pp. 513-524
    • Jiang, J.1    Prasad, K.2    Lafer, E.M.3    Sousa, R.4
  • 72
    • 34047268015 scopus 로고    scopus 로고
    • Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
    • Swain J.F., Dinler G., Sivendran R., Montgomery D.L., Stotz M., and Gierasch L.M. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol. Cell 26 (2007) 27-39
    • (2007) Mol. Cell , vol.26 , pp. 27-39
    • Swain, J.F.1    Dinler, G.2    Sivendran, R.3    Montgomery, D.L.4    Stotz, M.5    Gierasch, L.M.6
  • 73
    • 0041734594 scopus 로고    scopus 로고
    • Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ
    • Suh W.C., Lu C.Z., and Gross C.A. Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. 274 (1999) 30534-30539
    • (1999) J. Biol. Chem. , vol.274 , pp. 30534-30539
    • Suh, W.C.1    Lu, C.Z.2    Gross, C.A.3
  • 75
    • 0024600961 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins interact both in vivo and in vitro
    • Liberek K., Marszalek J., Ang D., Georgopoulos C., and Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins interact both in vivo and in vitro. J. Bacteriol. 171 (1991) 1590-1596
    • (1991) J. Bacteriol. , vol.171 , pp. 1590-1596
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 76
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?
    • Slepenkov S.V., and Witt S.N. The unfolding story of Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?. Mol. Microbiol. 45 (2002) 1197-1206
    • (2002) Mol. Microbiol. , vol.45 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 77
    • 31544442176 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones by a proline switch
    • Vogel M., Bukau B., and Mayer M.P. Allosteric regulation of Hsp70 chaperones by a proline switch. Mol. Cell 21 (2006) 359-367
    • (2006) Mol. Cell , vol.21 , pp. 359-367
    • Vogel, M.1    Bukau, B.2    Mayer, M.P.3
  • 78
    • 33846020582 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
    • Vogel M., Mayer M.P., and Bukau B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J. Biol. Chem. 281 (2006) 38705-38711
    • (2006) J. Biol. Chem. , vol.281 , pp. 38705-38711
    • Vogel, M.1    Mayer, M.P.2    Bukau, B.3
  • 79
    • 0025804392 scopus 로고
    • Characterization of the heat shock response in Lactococcus lactis subsp. lactis
    • Whitaker R.D., and Batt C.A. Characterization of the heat shock response in Lactococcus lactis subsp. lactis. Appl. Environ. Microbiol. 57 (1991) 1408-1412
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1408-1412
    • Whitaker, R.D.1    Batt, C.A.2
  • 80
    • 0029889975 scopus 로고    scopus 로고
    • Analysis of heat shock gene expression in Lactococcus lactis MG1363
    • Arnau J., Sørensen K.I., Appel K.F., Vogensen F.K., and Hammer K. Analysis of heat shock gene expression in Lactococcus lactis MG1363. Microbiology 142 (1996) 1685-1691
    • (1996) Microbiology , vol.142 , pp. 1685-1691
    • Arnau, J.1    Sørensen, K.I.2    Appel, K.F.3    Vogensen, F.K.4    Hammer, K.5
  • 81
    • 0141646554 scopus 로고    scopus 로고
    • Identification of proteins induced at low pH in Lactococcus lactis
    • Frees D., Vogensen F.K., and Ingmer H. Identification of proteins induced at low pH in Lactococcus lactis. Int. J. Food Microbiol. 87 (2003) 293-300
    • (2003) Int. J. Food Microbiol. , vol.87 , pp. 293-300
    • Frees, D.1    Vogensen, F.K.2    Ingmer, H.3
  • 83
    • 2442444147 scopus 로고    scopus 로고
    • Transcriptional analysis of the groE and dnaK heat-shock operons of Enterococcus faecalis
    • Laport M.S., Lemos J.A., Bastos C., Burne R.A., and Giambiagi-De Marval M. Transcriptional analysis of the groE and dnaK heat-shock operons of Enterococcus faecalis. Res. Microbiol. 155 (2004) 252-258
    • (2004) Res. Microbiol. , vol.155 , pp. 252-258
    • Laport, M.S.1    Lemos, J.A.2    Bastos, C.3    Burne, R.A.4    Giambiagi-De Marval, M.5
  • 84
    • 34247602112 scopus 로고    scopus 로고
    • Effects of prolonged exposure to alkaline pH on Enterococcus faecalis survival and specific gene transcripts
    • Appelbe O.K., and Sedgley C.M. Effects of prolonged exposure to alkaline pH on Enterococcus faecalis survival and specific gene transcripts. Oral Microbiol. Immunol. 22 (2007) 169-174
    • (2007) Oral Microbiol. Immunol. , vol.22 , pp. 169-174
    • Appelbe, O.K.1    Sedgley, C.M.2
  • 85
    • 0030944438 scopus 로고    scopus 로고
    • Alkaline stress response in Enterococcus faecalis: adaptation, cross-protection, and changes in protein synthesis
    • Flahaut S., Hartke A., Giard J.C., and Auffray Y. Alkaline stress response in Enterococcus faecalis: adaptation, cross-protection, and changes in protein synthesis. Appl. Environ. Microbiol. 63 (1997) 812-814
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 812-814
    • Flahaut, S.1    Hartke, A.2    Giard, J.C.3    Auffray, Y.4
  • 86
    • 0029978528 scopus 로고    scopus 로고
    • Relationship between stress response toward bile salts, acid and heat treatment in Enterococcus faecalis
    • Flahaut S., Hartke A., Giard J.C., Benachour A., Boutibonnes P., and Auffray Y. Relationship between stress response toward bile salts, acid and heat treatment in Enterococcus faecalis. FEMS Microbiol. Lett. 138 (1996) 49-54
    • (1996) FEMS Microbiol. Lett. , vol.138 , pp. 49-54
    • Flahaut, S.1    Hartke, A.2    Giard, J.C.3    Benachour, A.4    Boutibonnes, P.5    Auffray, Y.6
  • 88
    • 0037459148 scopus 로고    scopus 로고
    • HrcA is a negative regulator of the dnaK and groESL operons of Streptococcus pyogenes
    • Woodbury R., and Haldenwang W.G. HrcA is a negative regulator of the dnaK and groESL operons of Streptococcus pyogenes. Biochem. Biophys. Res. Commun. 302 (2003) 722-727
    • (2003) Biochem. Biophys. Res. Commun. , vol.302 , pp. 722-727
    • Woodbury, R.1    Haldenwang, W.G.2
  • 89
    • 0036249521 scopus 로고    scopus 로고
    • Analysis of Streptococcus mutans proteins modulated by culture under acidic conditions
    • Wilkins J.C., Homer K.A., and Beighton D. Analysis of Streptococcus mutans proteins modulated by culture under acidic conditions. Appl. Environ. Microbiol. 68 (2002) 2382-2390
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 2382-2390
    • Wilkins, J.C.1    Homer, K.A.2    Beighton, D.3
  • 90
    • 0029096159 scopus 로고
    • Expression of DnaK and GroEL homologs in Leuconostoc mesenteroides in response to heat shock, cold shock or chemical stress
    • Salotra P., Singh D.K., Seal K.P., Krishna N., Jaffe H., and Bhatnagar R. Expression of DnaK and GroEL homologs in Leuconostoc mesenteroides in response to heat shock, cold shock or chemical stress. FEMS Microbiol. Lett. 131 (1995) 57-62
    • (1995) FEMS Microbiol. Lett. , vol.131 , pp. 57-62
    • Salotra, P.1    Singh, D.K.2    Seal, K.P.3    Krishna, N.4    Jaffe, H.5    Bhatnagar, R.6
  • 91
    • 0036354638 scopus 로고    scopus 로고
    • Molecular characterization and regulatory analysis of dnaK operon of halophilic lactic acid bacterium Tetragenococcus halophila
    • Fukuda D., Watanabe M., Sonezaki S., Sugimoto S., Sonomoto K., and Ishizaki A. Molecular characterization and regulatory analysis of dnaK operon of halophilic lactic acid bacterium Tetragenococcus halophila. J. Biosci. Bioeng. 93 (2002) 388-394
    • (2002) J. Biosci. Bioeng. , vol.93 , pp. 388-394
    • Fukuda, D.1    Watanabe, M.2    Sonezaki, S.3    Sugimoto, S.4    Sonomoto, K.5    Ishizaki, A.6
  • 92
    • 0041375301 scopus 로고    scopus 로고
    • Effect of heterologous expression of molecular chaperone DnaK from Tetragenococcus halophilus on salinity adaptation of Escherichia coli
    • Sugimoto S., Nakayama J., Fukuda D., Sonezaki S., Watanabe M., Tosukhowong A., and Sonomoto K. Effect of heterologous expression of molecular chaperone DnaK from Tetragenococcus halophilus on salinity adaptation of Escherichia coli. J. Biosci. Bioeng. 96 (2003) 129-133
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 129-133
    • Sugimoto, S.1    Nakayama, J.2    Fukuda, D.3    Sonezaki, S.4    Watanabe, M.5    Tosukhowong, A.6    Sonomoto, K.7
  • 93
    • 41549164027 scopus 로고    scopus 로고
    • In vivo and in vitro complementation study comparing the function of DnaK chaperone systems from halophilic lactic acid bacterium Tetragenococcus halophilus and Escherichia coli
    • Sugimoto S., Saruwatari K., Higashi C., Tsuruno K., Matsumoto S., Nakayama J., and Sonomoto K. In vivo and in vitro complementation study comparing the function of DnaK chaperone systems from halophilic lactic acid bacterium Tetragenococcus halophilus and Escherichia coli. Biosci. Biotechnol. Biochem. 72 (2008) 811-822
    • (2008) Biosci. Biotechnol. Biochem. , vol.72 , pp. 811-822
    • Sugimoto, S.1    Saruwatari, K.2    Higashi, C.3    Tsuruno, K.4    Matsumoto, S.5    Nakayama, J.6    Sonomoto, K.7
  • 94
    • 34250338178 scopus 로고    scopus 로고
    • A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE
    • Sugimoto S., Higashi C., Saruwatari K., Nakayama J., and Sonomoto K. A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE. FEBS Lett. 581 (2007) 2993-2999
    • (2007) FEBS Lett. , vol.581 , pp. 2993-2999
    • Sugimoto, S.1    Higashi, C.2    Saruwatari, K.3    Nakayama, J.4    Sonomoto, K.5
  • 95
    • 0032956536 scopus 로고    scopus 로고
    • Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of Hsp70 suggest a novel outlook on phylogenies inferred from this protein
    • Gribaldo S., Lumia V., Creti R., de Macario E.C., Sanangelantoni A., and Cammarano P. Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of Hsp70 suggest a novel outlook on phylogenies inferred from this protein. J. Bacteriol. 181 (1999) 434-443
    • (1999) J. Bacteriol. , vol.181 , pp. 434-443
    • Gribaldo, S.1    Lumia, V.2    Creti, R.3    de Macario, E.C.4    Sanangelantoni, A.5    Cammarano, P.6
  • 96
    • 17644407779 scopus 로고    scopus 로고
    • The importance of having thermosensor control in the DnaK chaperone system
    • Siegenthaler R.K., and Christen P. The importance of having thermosensor control in the DnaK chaperone system. J. Biol. Chem. 280 (2005) 14395-14401
    • (2005) J. Biol. Chem. , vol.280 , pp. 14395-14401
    • Siegenthaler, R.K.1    Christen, P.2
  • 97
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüider S., Gemeroth L., Schneider-Mergener J., and Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16 (1997) 1501-1507
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüider, S.1    Gemeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 98
    • 4344590764 scopus 로고    scopus 로고
    • The J-protein family: modulating protein assembly, disassembly and translocation
    • Walsh P., Bursac D., Law Y.C., Cyr D., and Lithgow T. The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep. 5 (2004) 567-571
    • (2004) EMBO Rep. , vol.5 , pp. 567-571
    • Walsh, P.1    Bursac, D.2    Law, Y.C.3    Cyr, D.4    Lithgow, T.5
  • 99
    • 0032414399 scopus 로고    scopus 로고
    • The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-GrpE system
    • Silberg J.J., Hoff K.G., and Vickery L.E. The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-GrpE system. J. Bacteriol. 180 (1998) 6617-6624
    • (1998) J. Bacteriol. , vol.180 , pp. 6617-6624
    • Silberg, J.J.1    Hoff, K.G.2    Vickery, L.E.3
  • 100
    • 0034885052 scopus 로고    scopus 로고
    • + superfamily ATPases: common structure-diverse function
    • + superfamily ATPases: common structure-diverse function. Genes Cells 6 (2004) 575-597
    • (2004) Genes Cells , vol.6 , pp. 575-597
    • Ogura, T.1    Wilkinson, A.J.2
  • 103
    • 0037119995 scopus 로고    scopus 로고
    • The structure of bacterial DnaA: implication for general mechanisms underlying DNA replication initiation
    • Erzberger J.P., Pirruccello M.M., and Berger J.M. The structure of bacterial DnaA: implication for general mechanisms underlying DNA replication initiation. EMBO J. 21 (2002) 4763-4773
    • (2002) EMBO J. , vol.21 , pp. 4763-4773
    • Erzberger, J.P.1    Pirruccello, M.M.2    Berger, J.M.3
  • 104
    • 0037195418 scopus 로고    scopus 로고
    • Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease
    • Guo F., Maurizi M.R., Esser L., and Xia D. Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease. J. Biol. Chem. 277 (2002) 46743-46752
    • (2002) J. Biol. Chem. , vol.277 , pp. 46743-46752
    • Guo, F.1    Maurizi, M.R.2    Esser, L.3    Xia, D.4
  • 106
    • 0034502532 scopus 로고    scopus 로고
    • Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
    • Ortega J., Singh S.K., Ishikawa T., Maurizi M.R., and Steven A.C. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP. Mol. Cell 6 (2000) 1515-1521
    • (2000) Mol. Cell , vol.6 , pp. 1515-1521
    • Ortega, J.1    Singh, S.K.2    Ishikawa, T.3    Maurizi, M.R.4    Steven, A.C.5
  • 107
    • 0033681249 scopus 로고    scopus 로고
    • Crystal and solution structures of an HslUV protease-chaperone complex
    • Sousa M.C., Trame C.B., Tsuruta H., Wilbanks S.M., Reddy V.S., and McKay D.B. Crystal and solution structures of an HslUV protease-chaperone complex. Cell 103 (2000) 633-643
    • (2000) Cell , vol.103 , pp. 633-643
    • Sousa, M.C.1    Trame, C.B.2    Tsuruta, H.3    Wilbanks, S.M.4    Reddy, V.S.5    McKay, D.B.6
  • 108
    • 33747058216 scopus 로고    scopus 로고
    • A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases
    • Zolkiewski M. A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases. Mol. Microbiol. 61 (2006) 1094-1100
    • (2006) Mol. Microbiol. , vol.61 , pp. 1094-1100
    • Zolkiewski, M.1
  • 109
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon A., and Goldberg A.L. Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell 8 (2001) 1339-1349
    • (2001) Mol. Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 110
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., and Lindquist S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94 (1998) 73-82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 111
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK×J-GrpE set and ClpB chaperones
    • Motohashi K., Watanabe Y., Yohda M., and Yoshida M. Heat-inactivated proteins are rescued by the DnaK×J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. USA 96 (1999) 7184-7189
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 112
    • 0035093653 scopus 로고    scopus 로고
    • Characterization of Brucella suis clpB and clpAB mutants and participation of the genes in stress responses
    • Ekaza E., Teyssier J., Ouahrani-Bettache S., Liautard J.P., and Köhler S. Characterization of Brucella suis clpB and clpAB mutants and participation of the genes in stress responses. J. Bacteriol. 183 (2001) 2677-2681
    • (2001) J. Bacteriol. , vol.183 , pp. 2677-2681
    • Ekaza, E.1    Teyssier, J.2    Ouahrani-Bettache, S.3    Liautard, J.P.4    Köhler, S.5
  • 113
    • 0029785532 scopus 로고    scopus 로고
    • The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942
    • Eriksson M.J., and Clarke A.K. The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942. J. Bacteriol. 178 (1996) 4839-4846
    • (1996) J. Bacteriol. , vol.178 , pp. 4839-4846
    • Eriksson, M.J.1    Clarke, A.K.2
  • 114
    • 0029950703 scopus 로고    scopus 로고
    • Heat-shock protein 104 expression is sufficient for thermotolerance in yeast
    • Lindquist S., and Kim G. Heat-shock protein 104 expression is sufficient for thermotolerance in yeast. Proc. Natl. Acad. Sci. USA 93 (1996) 5301-5306
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5301-5306
    • Lindquist, S.1    Kim, G.2
  • 116
    • 10044227566 scopus 로고    scopus 로고
    • Hsp104 binds to yeast Sup35 prion fiber but needs other factor (s) to sever it
    • Inoue Y., Taguchi H., Kishimoto A., and Yoshida M. Hsp104 binds to yeast Sup35 prion fiber but needs other factor (s) to sever it. J. Biol. Chem. 279 (2004) 52319-52323
    • (2004) J. Biol. Chem. , vol.279 , pp. 52319-52323
    • Inoue, Y.1    Taguchi, H.2    Kishimoto, A.3    Yoshida, M.4
  • 117
    • 0032932216 scopus 로고    scopus 로고
    • Disruption and analysis of the clpB, clpC, and clpE genes in Lactococcus lactis: ClpE, a new Clp family in gram-positive bacteria
    • Ingmer H., Vogensen F.K., Hammer K., and Kilstrup M. Disruption and analysis of the clpB, clpC, and clpE genes in Lactococcus lactis: ClpE, a new Clp family in gram-positive bacteria. J. Bacteriol. 181 (1999) 2075-2083
    • (1999) J. Bacteriol. , vol.181 , pp. 2075-2083
    • Ingmer, H.1    Vogensen, F.K.2    Hammer, K.3    Kilstrup, M.4
  • 118
    • 1142298585 scopus 로고    scopus 로고
    • clpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance
    • Chastanet A., Derré I., Nair S., and Msadek T. clpB, a novel member of the Listeria monocytogenes CtsR regulon, is involved in virulence but not in general stress tolerance. J. Bacteriol. 186 (2004) 1165-1174
    • (2004) J. Bacteriol. , vol.186 , pp. 1165-1174
    • Chastanet, A.1    Derré, I.2    Nair, S.3    Msadek, T.4
  • 119
    • 0037329158 scopus 로고    scopus 로고
    • Comparative genomics reveal novel heat shock regulatory mechanisms in Staphylococcus aureus and other Gram-positive bacteria
    • Chastanet A., Fert J., and Msadek T. Comparative genomics reveal novel heat shock regulatory mechanisms in Staphylococcus aureus and other Gram-positive bacteria. Mol. Microbiol. 47 (2003) 1061-1073
    • (2003) Mol. Microbiol. , vol.47 , pp. 1061-1073
    • Chastanet, A.1    Fert, J.2    Msadek, T.3
  • 120
    • 10044275315 scopus 로고    scopus 로고
    • Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
    • Schlieker C., Tews I., Bukau B., and Mogk A. Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides. FEBS Lett. 578 (2004) 351-356
    • (2004) FEBS Lett. , vol.578 , pp. 351-356
    • Schlieker, C.1    Tews, I.2    Bukau, B.3    Mogk, A.4
  • 122
    • 40649098449 scopus 로고    scopus 로고
    • Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
    • Tessarz P., Mogk A., and Bukau B. Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol. Microbiol. 68 (2008) 87-97
    • (2008) Mol. Microbiol. , vol.68 , pp. 87-97
    • Tessarz, P.1    Mogk, A.2    Bukau, B.3
  • 123
    • 44849138934 scopus 로고    scopus 로고
    • Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
    • Haslberger T., Zdanowicz A., Brand I., Kirstein J., Turgay K., Mogk A., and Bukau B. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat. Struct. Mol. Biol. 15 (2008) 641-650
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 641-650
    • Haslberger, T.1    Zdanowicz, A.2    Brand, I.3    Kirstein, J.4    Turgay, K.5    Mogk, A.6    Bukau, B.7
  • 124
    • 33751579937 scopus 로고    scopus 로고
    • Structural and functional conversion of molecular chaperone ClpB from the gram-positive halophilic lactic acid bacterium Tetragenococcus halophilus mediated by ATP and stress
    • Sugimoto S., Yoshida H., Mizunoe Y., Tsuruno K., Nakayama J., and Sonomoto K. Structural and functional conversion of molecular chaperone ClpB from the gram-positive halophilic lactic acid bacterium Tetragenococcus halophilus mediated by ATP and stress. J. Bacteriol. 188 (2006) 8070-8078
    • (2006) J. Bacteriol. , vol.188 , pp. 8070-8078
    • Sugimoto, S.1    Yoshida, H.2    Mizunoe, Y.3    Tsuruno, K.4    Nakayama, J.5    Sonomoto, K.6
  • 126
    • 8144225912 scopus 로고    scopus 로고
    • Improved stress tolerance of GroESL-overproducing Lactococcus lactis and probiotic Lactobacillus paracasei NFBC 338
    • Desmond C., Fitzgerald G.F., Stanton C., and Ross R.P. Improved stress tolerance of GroESL-overproducing Lactococcus lactis and probiotic Lactobacillus paracasei NFBC 338. Appl. Environ. Microbiol. 70 (2004) 5929-5936
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5929-5936
    • Desmond, C.1    Fitzgerald, G.F.2    Stanton, C.3    Ross, R.P.4
  • 127
    • 0034919978 scopus 로고    scopus 로고
    • Improved acid tolerance of a recombinant strain of Escherichia coli expressing genes from the acidophilic bacterium Oenococcus oeni
    • Morel F., Delmas F., Jobin M.P., Diviès C., and Guzzo J. Improved acid tolerance of a recombinant strain of Escherichia coli expressing genes from the acidophilic bacterium Oenococcus oeni. Lett. Appl. Microbiol. 33 (2001) 126-130
    • (2001) Lett. Appl. Microbiol. , vol.33 , pp. 126-130
    • Morel, F.1    Delmas, F.2    Jobin, M.P.3    Diviès, C.4    Guzzo, J.5
  • 128
    • 36348946895 scopus 로고    scopus 로고
    • Improved adaptation to heat, cold, and solvent tolerance in Lactobacillus plantarum
    • Fiocco D., Capozzi V., Goffin P., Hols P., and Spano G. Improved adaptation to heat, cold, and solvent tolerance in Lactobacillus plantarum. Appl. Microbiol. Biotechnol. 77 (2007) 909-915
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 909-915
    • Fiocco, D.1    Capozzi, V.2    Goffin, P.3    Hols, P.4    Spano, G.5
  • 129
    • 0032523145 scopus 로고    scopus 로고
    • Molecular cloning, expression, and characterization of dnaK in Streptococcus pneumoniae
    • Kim S.W., Choi I.H., Kim S.N., Kim Y.H., Pyo S.N., and Rhee D.K. Molecular cloning, expression, and characterization of dnaK in Streptococcus pneumoniae. FEMS Microbiol. Lett. 161 (1998) 217-224
    • (1998) FEMS Microbiol. Lett. , vol.161 , pp. 217-224
    • Kim, S.W.1    Choi, I.H.2    Kim, S.N.3    Kim, Y.H.4    Pyo, S.N.5    Rhee, D.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.