메뉴 건너뛰기




Volumn 9, Issue 19, 1999, Pages

Protein folding: Who chaperones nascent chains in bacteria?

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS);

EID: 0033533704     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80467-9     Document Type: Note
Times cited : (15)

References (31)
  • 1
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl FU: Molecular chaperones in cellular protein folding. Nature 1996, 381:571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 2
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson JL, Craig EA: Protein folding in vivo: Unraveling complex pathways. Cell 1997, 90:201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 3
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau B, Horwich AL: The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92:351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 4
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu Z, Horwich AL, Sigler PB: The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 1997, 388:741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 5
    • 0027992757 scopus 로고
    • Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains
    • Kim S, Willison KR, Horwich AL: Cytosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains. Trends Biochem Sci 1994, 19:543-548.
    • (1994) Trends Biochem Sci , vol.19 , pp. 543-548
    • Kim, S.1    Willison, K.R.2    Horwich, A.L.3
  • 7
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann J, Horwich AL, Neupert W, Hartl FU: Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 1989, 341:125-130.
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.U.4
  • 8
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • Kang PJ, Ostermann J, Shilling J, Neupert W, Craig EA, Pfanner N: Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature 1990, 348:137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 10
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU: Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 1992, 356:683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 11
    • 0030928059 scopus 로고    scopus 로고
    • Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells
    • Eggers DK, Welch WJ, Hansen WJ: Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol Biol Cell 1997, 8:1559-1573.
    • (1997) Mol Biol Cell , vol.8 , pp. 1559-1573
    • Eggers, D.K.1    Welch, W.J.2    Hansen, W.J.3
  • 13
    • 0027980239 scopus 로고
    • A protein complex required for signal-sequence-specific sorting and translocation
    • Wiedmann B, Sakai H, Davis TA, Wiedmann M: A protein complex required for signal-sequence-specific sorting and translocation. Nature 1994, 370:434-440.
    • (1994) Nature , vol.370 , pp. 434-440
    • Wiedmann, B.1    Sakai, H.2    Davis, T.A.3    Wiedmann, M.4
  • 14
    • 0032573163 scopus 로고    scopus 로고
    • Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
    • Kim S, Schilke B, Craig EA, Horwich AL: Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci USA 1998, 95:12860-12865.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12860-12865
    • Kim, S.1    Schilke, B.2    Craig, E.A.3    Horwich, A.L.4
  • 16
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond C, Helenius A: Folding of VSV G protein: Sequential interaction with BiP and calnexin. Science 1994, 266:456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 17
    • 0033612301 scopus 로고    scopus 로고
    • The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70
    • Voisine C, Craig EA, Zufall N, von Ahsen O, Pfanner N, Voos W: The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70. Cell 1999, 97:565-574.
    • (1999) Cell , vol.97 , pp. 565-574
    • Voisine, C.1    Craig, E.A.2    Zufall, N.3    Von Ahsen, O.4    Pfanner, N.5    Voos, W.6
  • 18
    • 0023766740 scopus 로고
    • The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane
    • Lill R, Crooke E, Guthrie B, Wickner W: The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane. Cell 1988, 54:1013-1018.
    • (1988) Cell , vol.54 , pp. 1013-1018
    • Lill, R.1    Crooke, E.2    Guthrie, B.3    Wickner, W.4
  • 19
  • 20
    • 0028799459 scopus 로고
    • Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides
    • Valent QA, Kendall DA, High S, Kusters R, Bauke O, Luirink J: Early events in preprotein recognition in E. coli: Interaction of SRP and trigger factor with nascent polypeptides. EMBO J 1995, 14:5494-5505.
    • (1995) EMBO J , vol.14 , pp. 5494-5505
    • Valent, Q.A.1    Kendall, D.A.2    High, S.3    Kusters, R.4    Bauke, O.5    Luirink, J.6
  • 21
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • Hesterkamp T, Hauser S, Lütcke H, Bukau B: Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci USA 1996, 93:4437-4441.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lütcke, H.3    Bukau, B.4
  • 22
    • 0030881913 scopus 로고    scopus 로고
    • The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes
    • Hesterkamp T, Deuerling E, Bukau B: The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J Biol Chem 1997, 272:21865-21871.
    • (1997) J Biol Chem , vol.272 , pp. 21865-21871
    • Hesterkamp, T.1    Deuerling, E.2    Bukau, B.3
  • 23
    • 0000230763 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerases
    • Edited by Bukau B. Amsterdam: Harwood Academic Publ
    • Fischer G, Schmid FX: Peptidyl-prolyl cis/trans isomerases. In Molecular Chaperones and Folding Catalysts. Edited by Bukau B. Amsterdam: Harwood Academic Publ, 1999:461-489.
    • (1999) Molecular Chaperones and Folding Catalysts , pp. 461-489
    • Fischer, G.1    Schmid, F.X.2
  • 24
    • 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, Georgopoulos C: The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bacteriol 1989, 171:1379-1385.
    • (1989) J Bacteriol , vol.171 , pp. 1379-1385
    • Fayet, O.1    Ziegelhoffer, T.2    Georgopoulos, C.3
  • 25
    • 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: Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature 1999, 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
  • 27
    • 0030973119 scopus 로고    scopus 로고
    • Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures
    • Kandror O, Goldberg AL: Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures. Proc Natl Acad Sci USA 1997, 94:4978-4981.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4978-4981
    • Kandror, O.1    Goldberg, A.L.2
  • 28
    • 0032541496 scopus 로고    scopus 로고
    • Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli
    • Hesterkamp T, Bukau B: Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E. coli. EMBO J 1998, 17:4818-4828.
    • (1998) EMBO J , vol.17 , pp. 4818-4828
    • Hesterkamp, T.1    Bukau, B.2
  • 29
  • 30
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt KL, Hendrick JP, Houry WA, Hartl FU: In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 1997, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.