Nucleic Acids Research Advance Access originally published online on August 7, 2009
Nucleic Acids Research 2009 37(18):6116-6125; doi:10.1093/nar/gkp645
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Nucleic Acids Research, 2009, Vol. 37, No. 18 6116-6125
© 2009 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Stm1p alters the ribosome association of eukaryotic elongation factor 3 and affects translation elongation
Department of Molecular and Cellular Oncology, Unit 079, The University of Texas M. D. Anderson Cancer Center, 1515 Holcombe Boulevard, Houston, TX 77030-4009, USA
*To whom correspondence should be addressed. Tel: +1 713 792 8954; Fax: +1 713 794 3270; Email: mvandyke{at}mdanderson.org
Received March 12, 2009. Revised July 10, 2009. Accepted July 20, 2009.
Stm1p is a Saccharomyces cerevisiae protein that is primarily associated with cytosolic 80S ribosomes and polysomes. Several lines of evidence suggest that Stm1p plays a role in translation under nutrient stress conditions, although its mechanism of action is not yet known. In this study, we show that yeast lacking Stm1p (stm1
) are hypersensitive to the translation inhibitor anisomycin, which affects the peptidyl transferase reaction in translation elongation, but show little hypersensitivity to other translation inhibitors such as paromomycin and hygromycin B, which affect translation fidelity. Ribosomes isolated from stm1 yeast have intrinsically elevated levels of eukaryotic elongation factor 3 (eEF3) associated with them. Overexpression of eEF3 in cells lacking Stm1p results in a growth defect phenotype and increased anisomycin sensitivity. In addition, ribosomes with increased levels of Stm1p exhibit decreased association with eEF3. Taken together, our data indicate that Stm1p plays a complementary role to eEF3 in translation.