The Eukaryotic Translation Elongation Factor 1Bγ Has a Non-guanine Nucleotide Exchange Factor Role in Protein Metabolism

Document Type

Article

Publication Title

Journal of Biological Chemistry

Publication Date

12-3-2010

Abstract

The turnover of damaged proteins is critical to cell survival during stressful conditions such as heat shock or oxidative stress. The accumulation of misfolded proteins in the endoplasmic reticulum (ER) is toxic to cells. Therefore these proteins must be efficiently exported from the ER and degraded by the proteasome or the vacuole. Previously it was shown that the loss of eukaryotic elongation factor 1Bγ (eEF1Bγ) from the yeast Saccharomyces cerevisiae results in resistance to oxidative stress. Strains lacking eEF1Bγ show severe defects in protein turnover during conditions of oxidative stress. Furthermore, these strains accumulate a greater amount of oxidized proteins, which correlates with changes in heat shock chaperones. These strains show severe defects in vacuole morphology and defects related to the maturation of carboxypeptidase Y that is not dependent on the catalytic subunit of the eEF1B complex as a guanine nucleotide exchange factor. Finally, eEF1Bγ co-immunoprecipitates with an essential component of ER-Golgi transport vesicles. Taken together, these results support a broader protein metabolism role for eEF1Bγ.

Comments

This article was originally published as Esposito A.M. and Kinzy TG. (2010) The eukaryotic translation elongation factor 1B{gamma} has a non-guanine nucleotide exchange factor role in protein metabolism. J Biol Chem. 285:37995-8004. PMC2992233

DOI

10.1074/jbc.M110.160887

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