Identification of in vivo substrates of the chaperonin GroEL (original) (raw)
References
Georgopoulos,C. & Welch,W. J. Role of the major heat shock proteins as molecular chaperones. Annu. Rev. Cell Biol.9, 601–634 (1993). ArticleCAS Google Scholar
Ellis,R. J. Roles of molecular chaperones in protein folding. Curr. Opin. Struct. Biol.4, 117–122 (1994). ArticleCAS Google Scholar
Hartl,F. U. Molecular chaperones in cellular protein folding. Nature381, 571–580 (1996). ArticleADSCAS Google Scholar
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.171, 1379–1385 (1989). ArticleCAS Google Scholar
Horwich,A. L., Low,K. B., Fenton,W. A., Hirshfield,I. N. & Furtak,K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell74, 909–917 (1993). ArticleCAS Google Scholar
Fenton,W. A., Kashi,Y., Furtak,K. & Horwich,A. L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature371, 614–619 (1994). ArticleADSCAS Google Scholar
Coyle,J. E., Jaeger,J., Gross,M., Robinson,C. V. & Radford,S. E. Structural and mechanistic consequences of polypeptide binding by GroEL. Fold. Design2, R93–R104 (1997). ArticleCAS Google Scholar
Sigler,P. B. et al. Structure and function in GroEL-mediated protein folding. Annu., Rev. Biochem.67, 581–608 (1998). ArticleCAS Google Scholar
Ranson,N. A., White,H. E. & Saibil,H. R. Chaperonins. Biochem. J.333, 233–242 (1998). ArticleCAS Google Scholar
Ewalt,K. L., Hendrick,J. P., Houry,W. A. & Hartl,F. U. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell90, 491–500 (1997). ArticleCAS Google Scholar
Pedersen,S. Escherichia coli ribosomes translate in vivo with variable rate. EMBO J.3, 2895–2898 (1984). ArticleCAS Google Scholar
Xu,D. & Nussinov,R. Favorable domain size in proteins. Fold. Design3, 11–17 (1998). ArticleCAS Google Scholar
Xu,Z. H., Horwich,A. L. & Sigler,P. B. The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex. Nature388, 741–750 (1997). ArticleADSCAS Google Scholar
Ellis,R. J. & Hartl,F. U. Protein folding in the cell: Competing models of chaperonin function. FASEB J.10, 20–26 (1996). ArticleCAS Google Scholar
Rye,H. S. et al. GroEL–GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell97, 325–338 (1999). ArticleCAS Google Scholar
Ellis,R. J. Molecular chaperones: avoiding the crowd. Curr. Biol.7, R531–R533 (1997). ArticleCAS Google Scholar
Gentry,D. R. & Burgess,R. R. The cloning and sequence of the gene encoding the omega subunit of Escherichia coli RNA polymerase. Gene48, 33–40 (1986). ArticleCAS Google Scholar
Wada,M., Fujita,H. & Itikawa,H. Genetic suppression of a temperature-sensitive groES mutation by an altered subunit of RNA polymerase of Escherichia coli K-12. J. Bacteriol.169, 1102–1106 (1987). ArticleCAS Google Scholar
Ziemienowicz,A. et al. Both the Escherichia coli chaperone systems, GroEL/GroES and DnaK/DnaJ/GrpE, can reactivate heat-treated RNA polymerase. Different mechanisms for the same activity. J. Biol. Chem.268, 25425–25431 (1993). CASPubMed Google Scholar
VanBogelen,R. A., Sankar,P., Clark,R. L., Bogan,J. A. & Neidhardt,F. C. The gene–protein database of Escherichia coli: edition 5. Electrophoresis13, 1014–1054 (1992). ArticleCAS Google Scholar
Hubbard,T. J. P., Ailey,B., Brenner,S. E., Murzin,A. G. & Chothia,C. SCOP: a structural classification of proteins database. Nucleic Acids Res.27, 254–256 (1999). ArticleCAS Google Scholar
Orengo,C. A. et al. The CATH database provides insights into protein structure/function relationships. Nucleic Acids Res.27, 275–279 (1999). ArticleCAS Google Scholar
Eisenberg,D., Wilcox,W. & McLachlan,A. D. Hydrophobicity and amphiphilicity in protein structure. J. Cell. Biochem.31, 11–17 (1986). ArticleCAS Google Scholar
Cheng,M. Y. et al. Mitochondrial heat-shock protien hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature337, 620–625 (1989). ArticleADSCAS Google Scholar
Rye,H. S. et al. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature388, 792–798 (1997). ArticleADSCAS Google Scholar
Viitanen,P. V. et al. Chaperonin-facilitated refolding of the ribulsebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (GroEL) are K+ dependent. Biochemistry29, 5665–5671 (1990). ArticleCAS Google Scholar
Plaxco,K. W., Simons,K. T. & Baker,D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol.277, 985–994 (1998). ArticleCAS Google Scholar
Schlunegger,M. P., Bennett,M. J. & Eisenberg,D. Oligomer formation by 3D domain swapping: a model for protein assembly and misassembly. Adv. Protein Chem.50, 61–122 (1997). ArticleCAS Google Scholar
Landry,S. J., Jordan,R., McMacken,R. & Gierasch,L. M. Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature355, 455–457 (1992). ArticleADSCAS Google Scholar
Laminet,A. A., Ziegelhoffer,T., Georgopoulos,C. & Pluckthun,A. The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the beta-lactamase precursor. EMBO J.9, 2315–2319 (1990). ArticleCAS Google Scholar
Vitanen,P. V., Donaldson,G. K., Lorimer,G. H., Lubben,T. H. & Gatenby,A. A. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry30, 9716–9723 (1991). Article Google Scholar
Smith,K. E., Voziyan,P. A. & Fisher,M. T. Partitioning of rhodanese onto GroEL–chaperonin binds a reversibly oxidized form derived from the native protein. J. Biol. Chem.273, 28677–28681 (1998). ArticleCAS Google Scholar
Hayer-Hartl,M. K., Weber,F. & Hartl,F. U. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J.15, 6111–6121 (1996). ArticleCAS Google Scholar
Bjellqvist,B., Pasquali,C., Ravier,F., Sanchez,J. C. & Hochstrasser,D. A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale. Electrophoresis14, 1357–1365 (1993). ArticleCAS Google Scholar
Gorg,A., Postel,W. & Gunther,S. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis9, 531–546 (1988). ArticleCAS Google Scholar
Fountoulakis,M. & Langen,H. Identification of proteins by matrix-assisted laser desorption ionization-mass spectrometry following in-gel digestion in low-salt, nonvolatile buffer and simplified peptide recovery. Anal. Biochem.250, 153–156 (1997). ArticleCAS Google Scholar
Altschul,S. F. et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res.25, 3389–3402 (1997). ArticleCAS Google Scholar
Wootton,J. & Federhen,S. Statistics of local complexity in amino acid sequences and sequence databases. Comput. Chem.17, 149–163 (1993). ArticleCAS Google Scholar
Labedan,B. & Riley,M. Gene products of Escherichia coli: sequence comparisons and common ancestries. Mol. Biol. Evol.12, 980–987 (1995). CASPubMed Google Scholar
Klein,P., Kanehisa,M. & DeLisi,C. The detection and classification of membrane-spanning proteins. Biochim. Biophys. Acta815, 468–476 (1985). ArticleCAS Google Scholar
Frishman,D. & Argos,P. Seventy-five percent accuracy in protein secondary structure prediction. Proteins27, 329–335 (1997). ArticleCAS Google Scholar
Nakashima,H., Nishikawa,K. & Ooi,T. The folding type of a protein is relevant to the amino acid composition. J. Biochem.99, 153–162 (1986). ArticleCAS Google Scholar
Huynen,M. et al. Homology-based fold predictions for Mycoplasma genitalium proteins. J. Mol. Biol.280, 323–326 (1998). ArticleCAS Google Scholar
Frishman,D. & Mewes,H. W. Pedantic genome analysis. Trends Genet.13, 415–416 (1997). ArticleCAS Google Scholar
Bairoch,A. & Apweiler,R. The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1998. Nucleic Acids Res.26, 38–42 (1998). ArticleCAS Google Scholar
Karp,P. D., Riley,M., Paley,S. M., Pellegrini-Toole,A. & Krummenacker,M. EcoCyc: Encyclopedia of Escherichia coli genes and metabolism. Nucleic Acids Res.26, 50–53 (1998). ArticleCAS Google Scholar
Meyer,S. L. Data Analysis for Scientists and Engineers. (Wiley, New York, 1975).
Zhang,G. & Darst,S. A. Structure of the Escherichia coli RNA polymerase alpha subunit amino terminal domain. Science281, 262–266 (1998). ArticleADSCAS Google Scholar
Nicholls,A., Sharp,K. A. & Honig,B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins11, 281–296 (1991). ArticleCAS Google Scholar