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SSE1  -  adenyl-nucleotide exchange factor SSE1

Saccharomyces cerevisiae S288c

Synonyms: Chaperone protein MSI3, Heat shock protein homolog SSE1, LPG3, LPG3C, MSI3, ...
 
 
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Disease relevance of SSE1

  • Similarly, deletion of SSE1 causes a firefly luciferase folding defect in yeast cells under heat stress in vivo [1].
 

High impact information on SSE1

  • On the other hand, the absence of SSE1 enhances polypeptide binding to both SSB and SSA and impairs cell growth [2].
  • To test the in vivo requirement for interdomain communication, SSE1 alleles carrying amino acid substitutions in the ATPase domain were assayed for their ability to complement sse1Delta yeast [3].
  • To elucidate the mechanism of Ydj1p action, and to identify functional partners, we screened for multicopy suppressors of the temperature-sensitive ydj1-151 mutant and identified a yeast Hsp110, SSE1 [4].
  • Heat shock induction of SSE1, encoding a member of the Hsp110 family of heat shock proteins, was also dependent on the HSF CTA [5].
  • In this report, we demonstrate a novel synthetic genetic interaction between SSE1 and SCH9 [6].
 

Biological context of SSE1

 

Regulatory relationships of SSE1

 

Other interactions of SSE1

  • SSE1 and SSE2 are thought to encode polypeptides of 693 aa with calculated M(r)'s of 77,408 and 77,619, respectively [7].
  • The MSI3 gene was isolated as a multicopy suppressor of the heat shock-sensitive phenotype of the ira1 mutation, which causes hyperactivation of the RAS-cAMP pathway [8].

References

  1. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. Dragovic, Z., Broadley, S.A., Shomura, Y., Bracher, A., Hartl, F.U. EMBO J. (2006) [Pubmed]
  2. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. Yam, A.Y., Albanèse, V., Lin, H.T., Frydman, J. J. Biol. Chem. (2005) [Pubmed]
  3. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. Shaner, L., Trott, A., Goeckeler, J.L., Brodsky, J.L., Morano, K.A. J. Biol. Chem. (2004) [Pubmed]
  4. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity. Goeckeler, J.L., Stephens, A., Lee, P., Caplan, A.J., Brodsky, J.L. Mol. Biol. Cell (2002) [Pubmed]
  5. The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. Liu, X.D., Morano, K.A., Thiele, D.J. J. Biol. Chem. (1999) [Pubmed]
  6. The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae. Trott, A., Shaner, L., Morano, K.A. Genetics (2005) [Pubmed]
  7. Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family. Mukai, H., Kuno, T., Tanaka, H., Hirata, D., Miyakawa, T., Tanaka, C. Gene (1993) [Pubmed]
  8. MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae. Shirayama, M., Kawakami, K., Matsui, Y., Tanaka, K., Toh-e, A. Mol. Gen. Genet. (1993) [Pubmed]
 
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