Heat Shock pp 77-83 | Cite as

HSP70 Family of Proteins of the Yeast S. cerevisiae

  • E. Craig
  • P. J. Kang
  • W. Boorstein
Conference paper

Abstract

The most abundant heat shock protein in many organisms is a 70kDa protein called HSP70. In E. colithere is a single HSP70-related protein, the product of the dnaK gene. However, in most, if not all, eucaryotes, HSP70 is one of a family of related proteins. HSP70 families are usually composed of proteins that are expressed only after stress and those that are present under optimal growth conditions.

Keywords

Hydrolysis Urea Carboxyl Fractionation Polypeptide 

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References

  1. Boorstein, W and Craig, EA, Structure and regulation of the SSA4 gene of Saccharomyces cerevisiae. in press.Google Scholar
  2. Chappell, TG, Konforti, BB, Schmid, SLand Rothman, JE, (1987) The ATPase core of a clathrin uncoating protein. J. Biol. Chem., 262: 746–751.PubMedGoogle Scholar
  3. Cheng, M, Hartl, F-U, Martin, J, Pollock, R, Kalousek, F, Neupert, W, Hallberg, E, Hallberg, R and Horwich, A, (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature, 337: 620–625.PubMedCrossRefGoogle Scholar
  4. Craig, EA, (1985) The heat shock response. CRC Crit. Revs, in Biochem., 18: 239–280.Google Scholar
  5. Craig, EA and Jacobsen, K, (1985) Mutations in cognate gene of Saccharomyces cerevisiae HSP70 result in reduced growth rates at low temperatures. Mol. Cell Biol., 5: 3517–3524.PubMedGoogle Scholar
  6. Craig, EA, Kramer, J and Kosie-Smithers, J, (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.CrossRefGoogle Scholar
  7. Craig, EA, Kramer, J, Shilling, J, Werner-Washburne, M, Holmes, S, Kosic- Smither, J and Nicolet, CM, (1989) SSC1, an essential member of the S. cerevisiae HSP70 multigene family, encodes a mitochondrial protein. Mol Cell Biol., 9: 3000–3008.PubMedGoogle Scholar
  8. Craig, EA, Kang, PJ and Boorstein, W, (1990) A review of the role of 70kDa heat shoekproteins in protein translocation across membranes Ant van Leeuw Intl. J. Gen. Mol. Microbiol., 58: 137–146.Google Scholar
  9. Deshaies, R, Koch, B, Werner-Washburne, M, Craig, E and Sehekman, R (1988) A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature, 332: 800–805.PubMedCrossRefGoogle Scholar
  10. Engman, D, Kirchhoff, LV and Donelson, JE, (1989) Molecular cloning of mtp70, a mitochondrial member of the HSP70 family. Mol. Cell Biol., 9: 5163–5168.PubMedGoogle Scholar
  11. Flynn, GC, Chappell, TG and Rothman, JE, (1989) Peptide binding and release by proteins implicated as catalysts of protein assembly. Science, 245: 385–390.PubMedCrossRefGoogle Scholar
  12. Hartl, F-U and Neupert, W, (1990) Protein sorting to mitochondria: Evolutionary conservations of folding and assembly. Science, 247: 930–938.PubMedCrossRefGoogle Scholar
  13. Kang, PJ, Osterman, J, Shilling, J, Neupert, W, Craig, EA and Pfanner, N, (1990) Requirements for HSP70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature (London), 348: 137–143.CrossRefGoogle Scholar
  14. Leustek, T, Dalie, B, Amir-Shapira, D, Brot, N and Weissbach, H, (1989) A member of the hsp70 family is localized in mitochondria and resembles Escherichia coli DnaK. Proc. Natl. Acad. Sci. USA, 86: 7805–7808.CrossRefGoogle Scholar
  15. Lindquist, S, (1986) The heat-shock response. Ann. Rev. Biochem., 55: 1151–1191.PubMedCrossRefGoogle Scholar
  16. Mizzen, LA, Chang, C, Garrels, JI and Welch, W, (1989) Identification, characterization, and purification of two mammalian stress proteins present in mitochondria: One related to HSP70, the other to GroEL. 264: 20664–20675.Google Scholar
  17. Munro, S and Pelham, HRB, (1986) An hsp70-like protein in the ER: Identity with the 78kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell, 46: 291–300.PubMedCrossRefGoogle Scholar
  18. Ostermann, J, Horwich, AL, Neupert, Wand Hartl, F-U, (1989) Protein foldingin mitochondria requires complex formation with HSP60 and ATP hydrolysis. Nature, 341: 125–130.PubMedCrossRefGoogle Scholar
  19. Rose, MD, Misra, LM and Vogel, JP, (1989) KAR2, a kaiyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell, 57: 1211–1221PubMedCrossRefGoogle Scholar
  20. Rothman, J, (1989) Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells. Cell, 59 (135): 591–601.PubMedCrossRefGoogle Scholar
  21. Slater, MR and Craig, EA (1989) The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae. Nucl. Acid. Res., 17 (79): 805–806.CrossRefGoogle Scholar
  22. Vogel, JP, Misra, LM and Rose, MD (1990) Loss of BiP/grp78 function blocks translocation of secretory proteins in yeast. J. Cell Biol., 110: 1885–1895.PubMedCrossRefGoogle Scholar
  23. Welch, W and Feramisco, J, (1984) Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J Biol. Chem., 259: 4501–4513.PubMedGoogle Scholar
  24. Werner-Washburne, M, Stone, DE and Craig, EA, (1987) Complex interactions among members of an essential subfamily of HSP70 genes in Saccharomyces cerevisiae. Mol. Cell Biol., 7: 2568–2577.PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1991

Authors and Affiliations

  • E. Craig
    • 1
  • P. J. Kang
    • 1
  • W. Boorstein
    • 1
  1. 1.Department of Physiological ChemistryUniversity of Wisconsin-MadisonMadison, WisconsinUSA

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