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Gene Review

SBH1  -  Sbh1p

Saccharomyces cerevisiae S288c

Synonyms: Protein transport protein SBH1, SEB1, Sec61 complex subunit SBH1, Sec61 complex subunit beta, YER087BC, ...
 
 
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High impact information on SBH1

  • Sbh1p and Sbh2p individually are also not essential, but cells lacking both proteins are impaired in their growth at elevated temperatures and accumulate precursors of secretory proteins; microsomes isolated from these cells also exhibit a reduced rate of post-translational protein transport [1].
  • Previously, we identified SEB1/SBH1, encoding the beta subunit of the Sec61p ER translocation complex, as a multicopy suppressor of the sec15-1 mutant, defective for one subunit of the exocyst complex [2].
  • Furthermore, in wild type cells overexpression of SEB1 as well as SEC4 resulted in increased production of secreted proteins [2].
  • The GenBank Accession Nos are AF307983 (K. lactis SSO1) and AF318314 (K. lactis SEB1) [3].
  • The SEB1/SBH1 and the SSO genes encode components of the protein secretory machinery functioning at the opposite ends, ER translocation and exocytosis, respectively, of the secretory pathway in Saccharomyces cerevisiae [3].
 

Biological context of SBH1

  • Overexpression of SEB1 from a multicopy plasmid suppressed the temperature sensitivity of sec61-2 and sec61-3 mutants [4].
  • Disruption of the chromosomal SEB2 was not lethal whereas the double disruption of SEB1 and SEB2 resulted in a temperature-sensitive phenotype [4].
  • The Trichoderma atroviride seb1 (stress response element binding) gene encodes an AGGGG-binding protein which is involved in the response to high osmolarity stress [5].
  • The S.pombe protein, named Seb1 for seven binding, was essential for cell viability, and bound directly to Rpb7 in vitro [6].
 

Anatomical context of SBH1

  • Secretory proteins are translocated across the endoplasmic reticulum (ER) membrane through a channel formed by three proteins, namely Sec61p, Sbh1p, and Sss1p (Johnson, A. E., and van Waes, M. A. (1999) Annu. Rev. Cell Dev. Biol. 15, 799-842) [7].
  • The in vitro translated Seb1p was post-translationally inserted into microsomal membranes [4].
 

Associations of SBH1 with chemical compounds

  • Levels of seb1 mRNA increased under conditions of osmotic stress (sorbitol, NaCl) but not under other stress conditions (cadmium sulfate, pH, membrane perturbance) [5].
 

Analytical, diagnostic and therapeutic context of SBH1

References

  1. A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. Finke, K., Plath, K., Panzner, S., Prehn, S., Rapoport, T.A., Hartmann, E., Sommer, T. EMBO J. (1996) [Pubmed]
  2. The beta subunit of the Sec61p endoplasmic reticulum translocon interacts with the exocyst complex in Saccharomyces cerevisiae. Toikkanen, J.H., Miller, K.J., Söderlund, H., Jäntti, J., Keränen, S. J. Biol. Chem. (2003) [Pubmed]
  3. Kluyveromyces lactis SSO1 and SEB1 genes are functional in Saccharomyces cerevisiae and enhance production of secreted proteins when overexpressed. Toikkanen, J.H., Sundqvist, L., Keränen, S. Yeast (2004) [Pubmed]
  4. Yeast protein translocation complex: isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 beta subunit. Toikkanen, J., Gatti, E., Takei, K., Saloheimo, M., Olkkonen, V.M., Söderlund, H., De Camilli, P., Keränen, S. Yeast (1996) [Pubmed]
  5. The Trichoderma atroviride seb1 (stress response element binding) gene encodes an AGGGG-binding protein which is involved in the response to high osmolarity stress. Peterbauer, C.K., Litscher, D., Kubicek, C.P. Mol. Genet. Genomics (2002) [Pubmed]
  6. Rpb7 subunit of RNA polymerase II interacts with an RNA-binding protein involved in processing of transcripts. Mitsuzawa, H., Kanda, E., Ishihama, A. Nucleic Acids Res. (2003) [Pubmed]
  7. Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein. Scheper, W., Thaminy, S., Kais, S., Stagljar, I., Römisch, K. J. Biol. Chem. (2003) [Pubmed]
 
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