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Gene Review

LHS1  -  Hsp70 family chaperone LHS1

Saccharomyces cerevisiae S288c

Synonyms: CER1, Heat shock protein 70 homolog LHS1, SSI1, YKL073W, YKL355
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Disease relevance of LHS1

  • Lhs1p may be part of a fundamental heat-resistant survival machinery needed for recovery of yeast cells from severe heat stress [1].

High impact information on LHS1


Biological context of LHS1


Associations of LHS1 with chemical compounds

  • However, deletion of SSI1 results in cold sensitivity as well as enhanced resistance to manganese [5].
  • Like KAR2, SSI1 is induced both in the presence of tunicamycin and in a kar2-159 mutant strain, conditions which lead to an accumulation of unfolded proteins in the ER [5].
  • Lhs1p stimulated Kar2p by providing a specific nucleotide exchange activity, whereas Kar2p reciprocally activated the Lhs1p adenosine triphosphatase (ATPase) [6].

Physical interactions of LHS1

  • Deletion of SSI1 shows a complex pattern of genetic interactions with various conditional alleles of KAR2, ranging from synthetic lethality to synthetic rescue [5].

Other interactions of LHS1

  • Refolding of cytoplasmic proteins requires the Hsp104 chaperone, and refolding of lumenal endoplasmic reticulum (ER) proteins requires the Hsp70 homologue Lhs1p [7].
  • Here we show that the endoplasmic reticulum (ER) chaperones BiP/Kar2p and Lhs1p and the mitochondrial chaperone Hsp78 were also upregulated at the physiological temperature during recovery from thermal insult [8].


  1. The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. Saris, N., Holkeri, H., Craven, R.A., Stirling, C.J., Makarow, M. J. Cell Biol. (1997) [Pubmed]
  2. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. Tyson, J.R., Stirling, C.J. EMBO J. (2000) [Pubmed]
  3. A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum. Dierks, T., Volkmer, J., Schlenstedt, G., Jung, C., Sandholzer, U., Zachmann, K., Schlotterhose, P., Neifer, K., Schmidt, B., Zimmermann, R. EMBO J. (1996) [Pubmed]
  4. Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae. Hamilton, T.G., Norris, T.B., Tsuruda, P.R., Flynn, G.C. Mol. Cell. Biol. (1999) [Pubmed]
  5. SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum. Baxter, B.K., James, P., Evans, T., Craig, E.A. Mol. Cell. Biol. (1996) [Pubmed]
  6. Coordinated activation of Hsp70 chaperones. Steel, G.J., Fullerton, D.M., Tyson, J.R., Stirling, C.J. Science (2004) [Pubmed]
  7. The cytoplasmic chaperone hsp104 is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum. Hänninen, A.L., Simola, M., Saris, N., Makarow, M. Mol. Biol. Cell (1999) [Pubmed]
  8. Regulation and recovery of functions of Saccharomyces cerevisiae chaperone BiP/Kar2p after thermal insult. Seppä, L., Makarow, M. Eukaryotic Cell (2005) [Pubmed]
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