REFERENCES
- Atencio, D. P., and J. Yaffe 1992. MAS5, a yeast homolog of DnaJ involved in mitochondrial protein import. Mol. Cell. Biol. 12:283–291.
- Ausubel, F., R. Brent, R. Kingston, D. Moore, J. G. Seidman, J. Smith, K. Struhl 1997. Current protocols in molecular biology. John Wiley and Sons, New York, N.Y.
- Becker, J., W. Walter, W. Yan, and J. Craig 1996. Functional interaction of cytosolic Hsp70 and DnaJ-related protein, Ydj1p, in protein translocation in vivo. Mol. Cell. Biol. 16:4378–4386.
- Buchberger, A., J. Reinstein, B. Bukau 1999. The DnaK chaperone system: mechanism and comparison with other Hsp70 systems, p. 609–635. In B. Bukau (ed.), Molecular chaperones and folding catalysts: regulation, cellular function and mechanisms. Harwood Academic Publishers, Amsterdam, The Netherlands.
- Bukau, B., F. X. Schmid, J. Buchner 1999. Assisted protein folding, p. 3–10. In B. Bukau (ed.), Molecular chaperones and folding catalysts: regulation, cellular function and mechanisms. Harwood Academic Publishers, Amsterdam, The Netherlands.
- Caplan, A. J., D. M. Cyr, and J. Douglas 1992. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71:1143–1155.
- Caplan, A. J., and J. Douglas 1991. Characterization of YDJ1: a yeast homologue of the bacterial DnaJ protein. J. Cell Biol. 114:609–621.
- Caplan, A. J., J. Tsai, P. J. Casey, and J. Douglas 1992. Farnesylation of YDJ1p is required for function at elevated growth temperatures in S. cerevisiae. J. Biol. Chem. 267:18890–18895.
- Cheetham, M., and J. Caplan 1998. Structure, function and evolution of DnaJ: conservation and adaption of chaperone function. Cell Stress Chaperones 3:28–36.
- Craig, E., W. Yan, P. James 1999. Genetic dissection of the Hsp70 chaperone system of yeast, p. 139–162. In B. Bukau (ed.), Molecular chaperones and folding catalysts: regulation, cellular function and mechanisms. Harwood Academic Publishers, Amsterdam, The Netherlands.
- Dey, B., A. J. Caplan, and J. Boschelli 1996. The Ydj1 molecular chaperone facilitates formation of active p60v-src in yeast. Mol. Biol. Cell 7:91–100.
- Feldheim, D., J. Rothblatt, and J. Schekman 1992. Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation. Mol. Cell. Biol. 12:3288–3296.
- Greene, M., K. Maskos, and J. Landry 1998. Role of the J-domain in the cooperation of Hsp40 with Hsp70. Proc. Natl. Acad. Sci. USA 95:6108–6113.
- Hartl, F. U. 1996. Molecular chaperones in cellular protein folding. Nature 381:571–580.
- Hettema, E. H., C. C. M. Ruigrok, M. G. Koerkamp, M. v. d. Berg, H. F. Tabak, B. Distel, and J. Braakman 1998. The cytosolic DnaJ-like protein Djp1p is involved specifically in peroxisomal protein import. J. Cell Biol. 142:421–434.
- Horton, L., and J. Hensold. Personal communication.
- Huang, K., J. M. Flanagan, and J. Prestegard 1999. The influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJ. Protein Sci. 8:203–214.
- Johnson, J., and E. Craig. Unpublished data.
- Karzai, A. W., and J. McMacken 1996. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271:11236–11246.
- Kelley, W. L. 1998. The J-domain family and the recruitment of chaperone power. Trends Biochem. 23:222–227.
- Laufen, T., M. Mayer, C. Beisel, D. Klostermeier, A. Mogk, J. Reinstein, and J. Bukau 1999. Mechanism of regulation of Hsp70 chaperones by DnaJ co-chaperones. Proc. Natl. Acad. Sci. USA 96:5452–5457.
- Lu, Z., and J. Cyr 1998. Protein folding activity of Hsp70 is modified differently by the Hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 273:27824–27830.
- Lu, Z., and J. Cyr 1998. The conserved carboxyl terminus and zinc finger-like domain of the co-chaperone Ydj1 assist Hsp70 in protein folding. J. Biol. Chem. 273:5970–5978.
- Luke, M., A. Suttin, and J. Arndt 1991. Characterization of SIS1, a Saccharomyces cerevisiae homologue of bacterial dnaJ proteins. J. Cell Biol. 114:623–638.
- Misselwitz, B., O. Staeck, and J. Rapoport 1998. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol. Cell 2:593–603.
- Mumberg, D., R. Muller, and J. Funk 1995. Yeast vectors for the controlled expression of heterologous proteins in different genetic backgrounds. Gene 156:119–122.
- Pellecchia, M., T. Szyperski, D. Wall, C. Georgopoulos, and J. Wuthrich 1996. NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone. J. Mol. Biol. 260:236–250.
- Pfund, C., N. Lopez-Hoyo, T. Ziegelhoffer, B. A. Schilke, P. Lopez-Buesa, W. A. Walter, M. Wiedmann, and J. Craig 1998. The molecular chaperone SSB from S. cerevisiae is a component of the ribosome-nascent chain complex. EMBO J. 17:3981–3989.
- Qian, Y. Q., D. Patel, F. U. Hartl, and J. McColl 1996. Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J. Mol. Biol. 260:224–235.
- Rothstein, R. 1991. Targeting, disruption, replacement and allele rescue: intergrative DNA transformation in yeast. Methods Enzymol. 194:281–301.
- Schlenstedt, G., S. Harris, B. Risse, R. Lill, and J. Silver 1995. A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J. Cell Biol. 129:979–988.
- Schmid, D., A. Baici, H. Gehring, and J. Christen 1994. Kinetics of molecular chaperone action. Science 263:971–973.
- Sherman, F., G. R. Fink, J. B. Hicks 1986. Laboratory course manual for methods in yeast genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
- Sikorski, R. S., and J. Boeke 1991. In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol. 194:302–318.
- Sikorski, R. S., and J. Hieter 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19–27.
- Silver, P. A., and J. Way 1993. Eukaryotic DnaJ homologs and the specificity of Hsp70 activity. Cell 74:5–6.
- Strain, J., C. R. Lorenz, J. Bode, S. Garland, G. A. Smolen, D. T. Ta, L. E. Vickery, and J. Culotta 1998. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. J. Biol. Chem. 273:31138–31144.
- Suh, W.-C., W. Burkholder, C. Z. Lu, X. Zhao, M. Gottesman, and J. Gross 1998. Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Proc. Natl. Acad. Sci. USA 95:15223–15228.
- Tsai, J., and J. Douglas 1996. A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271:9347–9354.
- Voisine, C., and E. Craig. Unpublished results.
- Wall, D., M. Zylicz, and J. Georgopoulos 1995. The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J. Biol. Chem. 270:2139–2144.
- Wall, D., M. Zylicz, and J. Georgopoulos 1994. The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. J. Biol. Chem. 269:5446–5451.
- Westermann, B., and J. Neupert 1997. Mdj2p, a novel DnaJ homolog in the mitochondrial inner membrane of the yeast. J. Mol. Biol. 272:477–483.
- Yan, W., B. Schilke, C. Pfund, W. Walter, S. Kim, and J. Craig 1998. Zuotin, a ribosome-associated DnaJ molecular chaperone. EMBO J. 17:4809–4817.
- Zhong, T., and J. Arndt 1993. The yeast SIS1 protein, a DnaJ homolog, is required for initiation of translation. Cell 73:1175–1186.
- Ziegelhoffer, T., P. Lopez-Buesa, and J. Craig 1995. The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J. Biol. Chem. 270:10412–10419.