Mitochondrial GrpE Is Present in a Complex with hsp70 and Preproteins in Transit across Membranes

REFERENCES

• Ang, D., K. Liberek, D. Skowyra, M. Zylicz, and C. Georgopoulos. 1991. Biological role and regulation of the universally conserved heat shock proteins. J. Biol. Chem. 266:24233–24236.
   PubMed Web of Science ®Google Scholar
• Blom, J., M. Kübrich, J. Rassow, W. Voos, P. J. T. Dekker, A. C. Maarse, M. Meijer, and N. Pfanner. 1993. The essential yeast protein MIM44 (encoded by MPI1) is involved in an early step of preprotein translocation across the mitochondrial inner membrane. Mol. Cell. Biol. 13:7364–7371.
   PubMedGoogle Scholar
• Blumberg, H., and P. A. Silver. 1991. A homologue of the bacterial heat-shock gene DnaJ that alters protein sorting in yeast. Nature (London) 349:627–630.
   PubMedGoogle Scholar
• Brodsky, J. L., and R. Schekman. 1993. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J. Cell Biol. 123:1355–1363.
   PubMed Web of Science ®Google Scholar
• Craig, E. A., J. Kramer, and J. Kosic-Smithers. 1987. SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth. Proc. Natl. Acad. Sci. USA 84:4156–4160.
   PubMed Web of Science ®Google Scholar
• Cyr, D., X. Lu, and M. Douglas. 1992. Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267:20927–20931.
   PubMed Web of Science ®Google Scholar
• Daum, G., S. M. Gasser, and G. Schatz. 1982. Import of proteins into mitochondria: energy-dependent, two-step processing of the intermembrane space enzyme cytochrome b2 by isolated mitochondria. J. Biol. Chem. 257:13075–13080.
   PubMed Web of Science ®Google Scholar
• Eilers, M., and G. Schatz. 1986. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature (London) 322:228–232.
   PubMedGoogle Scholar
• Gambill, B. D., W. Voos, P. J. Kang, B. Miao, T. Langer, E. A. Craig, and N. Pfanner. 1993. A dual role for mitochondrial heat shock protein 70 in membrane translocation of preproteins. J. Cell Biol. 123:109–117.
   PubMed Web of Science ®Google Scholar
• Gamer, J., H. Bujard, and B. Bukau. 1992. Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor σ32. Cell 69:833–842.
   PubMedGoogle Scholar
• Georgopoulos, C. 1992. The emergence of the chaperone machines. Trends Biochem. Sci. 17:295–299.
   PubMedGoogle Scholar
• Hartl, F.-U., R. Hlodan, and T. Langer. 1994. Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem. Sci. 19:20–25.
   PubMed Web of Science ®Google Scholar
• Hartl, F.-U., J. Ostermann, B. Guiard, and W. Neupert. 1987. Successive translocation into and out of the mitochondrial matrix: targeting of proteins to the intermembrane space by a bipartite signal peptide. Cell 51:1027–1037.
   PubMed Web of Science ®Google Scholar
• Hartl, F.-U., B. Schmidt, E. Wachter, H. Weiss, and W. Neupert. 1986. Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase. Cell 47:939–951.
   PubMed Web of Science ®Google Scholar
• Ikeda, E., S. Yoshida, H. Mitsuzawa, I. Uno, and A. Toh-e. 1994. YGE1 is a yeast homologue of Escherichia coligrpE and is required for maintenance of mitochondrial functions. FEBS Lett. 339:265–268.
   PubMedGoogle Scholar
• Kambouris, N. G., D. J. Burke, and C. E. Creutz. 1993. Cloning and genetic analysis of the gene encoding a new protein kinase in Saccharomyces cerevisiae. Yeast 9:141–150.
   PubMedGoogle Scholar
• Kang, P. J., J. Ostermann, J. Shilling, W. Neupert, E. A. Craig, and N. Pfanner. 1990. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature (London) 348:137–143.
   PubMed Web of Science ®Google Scholar
• Koll, Η., B. Guiard, J. Rassow, J. Ostermann, A. L. Horwich, W. Neupert, and F.-U. Hartl. 1992. Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space. Cell 68:1163–1175.
   PubMed Web of Science ®Google Scholar
• Laloraya, S., B. D. Gambill, and E. A. Craig. 1994. A role for a eukaryotic grpE-related protein, Mge1p, in protein translocation. Proc. Natl. Acad. Sci. USA 91:6481–6485.
   PubMed Web of Science ®Google Scholar
• Langer, T., C. Lu, H. Echols, J. Flanagan, M. K. Hayer-Hartl, and F.-U. Hartl. 1992. Successive action of DnaK (Hsp70), DnaJ, and GroEL (Hsp60) along the pathway of chaperone-assisted protein folding. Nature (London) 356:683–689.
   PubMed Web of Science ®Google Scholar
• Liberek, K., J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88:2874–2878.
   PubMed Web of Science ®Google Scholar
• Manning-Krieg, U. C., P. E. Scherer, and G. Schatz. 1991. Sequential action of mitochondrial chaperones in protein import into mitochondria. EMBO J. 10:3273–3280.
   PubMedGoogle Scholar
• Osipiuk, J., C. Georgopoulos, and M. Zylicz. 1993. Initiation of lambda DNA replication. The Escherichia coli small heat shock proteins, DnaJ and GrpE, increase DnaK's affinity for the lambda P protein. J. Biol. Chem. 268:4821–4827.
   PubMedGoogle Scholar
• Ostermann, J., W. Voos, P. J. Kang, E. A. Craig, W. Neupert, and N. Pfanner. 1990. Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix. FEBS Lett. 277:281–284.
   PubMed Web of Science ®Google Scholar
• Perrin, D. D., and B. Dempsey. 1974. Buffers for pH and metal ion control, p. 96–99. Chapman and Hall Ltd., London.
   Google Scholar
• Pfanner, N., Η. K. Muller, M. A. Harmey, and W. Neupert. 1987. Mitochondrial protein import: involvement of the mature part of a cleavable precursor protein in the binding to receptor sites. EMBO J. 6:3449–3454.
   PubMedGoogle Scholar
• Pfanner, N., and W. Neupert. 1985. Transport of proteins into mitochondria: a potassium diffusion potential is able to drive the import of the ADP/ATP carrier. EMBO J. 4:2819–2825.
   PubMedGoogle Scholar
• Pfanner, N., M. Tropschug, and W. Neupert. 1987. Mitochondrial protein import: nucleoside triphosphates are involved in conferring import-competence to precursors. Cell 49:815–823.
   PubMedGoogle Scholar
• Rassow, J., B. Guiard, U. Wienhues, V. Herzog, F.-U. Hartl, and W. Neupert. 1989. Translocation arrest by reversible folding of a precursor protein imported into mitochondria. A means to quantitate translocation contact sites. J. Cell Biol. 109:1421–1428.
   PubMed Web of Science ®Google Scholar
• Scherer, P. E., U. C. Krieg, S. T. Hwang, D. Vestweber, and G. Schatz. 1990. A precursor protein partly translocated into yeast mitochondria is bound to a 70 kD mitochondrial stress protein. EMBO J. 9:4315–4322.
   PubMedGoogle Scholar
• Schleyer, M., B. Schmidt, and W. Neupert. 1982. Requirement of a membrane potential for the postranslational transfer of proteins into mitochondria. Eur. J. Biochem. 125:109–116.
   PubMedGoogle Scholar
• Schwaiger, M., V. Herzog, and W. Neupert. 1987. Characterization of translocation contact sites involved in the import of mitochondrial proteins. J. Cell Biol. 105:235–246.
   PubMed Web of Science ®Google Scholar
• Schwarz, E., T. Seytter, B. Guiard, and W. Neupert. 1993. Targeting of cytochrome b2 into the mitochondrial intermembrane space: specific recognition of the sorting signal. EMBO J. 12:2295–2302.
   PubMedGoogle Scholar
• Sherman, M. Y., and A. L. Goldberg. 1991. Formation in vitro of complexes between an abnormal fusion protein and the heat shock proteins from Escherichia coli and yeast mitochondria. J. Bacteriol. 173:7249–7256.
   PubMedGoogle Scholar
• Skowyra, D., and S. Wickner. 1993. The interplay of the GrpE heat shock protein and Mg2+ in RepA monomerization by DnaJ and DnaK. J. Biol. Chem. 268:25296–25301.
   PubMedGoogle Scholar
• Söllner, T., J. Rassow, and N. Pfanner. 1991. Analysis of mitochondrial protein import using translocation intermediates and specific antibodies. Methods Cell Biol. 34:345–358.
   PubMedGoogle Scholar
• Stuart, R. A., D. M. Cyr, E. A. Craig, and W. Neupert. 1994. Mitochondrial molecular chaperones: their role in protein translocation. Trends Biochem. Sci. 19:87–92.
   PubMedGoogle Scholar
• Voos, W., B. D. Gambill, B. Guiard, N. Pfanner, and E. A. Craig. 1993. Presequence and mature part of preproteins strongly influence the dependence of mitochondrial protein import on heat shock protein 70 in the matrix. J. Cell Biol. 123:119–126.
   PubMed Web of Science ®Google Scholar
• Zylicz, M. 1993. The Escherichia coli chaperones involved in DNA replication. Philos. Trans. R. Soc. Lond. B 339:271–277.
   PubMedGoogle Scholar
• Zylicz, M., and D. G. Ang. 1987. The grpE protein of Escherichia coli. J. Biol. Chem. 262:17437–17442.
   PubMed Web of Science ®Google Scholar