This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Holmes, L. E. A.
Right arrow Articles by Ashe, M. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Holmes, L. E. A.
Right arrow Articles by Ashe, M. P.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2004, p. 2998-3010, Vol. 24, No. 7
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.7.2998-3010.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Loss of Translational Control in Yeast Compromised for the Major mRNA Decay Pathway

L. E. A. Holmes,1 S. G. Campbell,1 S. K. De Long,2 A. B. Sachs,2 and M. P. Ashe1*

Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, Manchester M60 1QD, United Kingdom,1 Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, California 947202

Received 8 October 2003/ Returned for modification 12 November 2003/ Accepted 15 January 2004

The cytoplasmic fate of mRNAs is dictated by the relative activities of the intimately connected mRNA decay and translation initiation pathways. In this study, we have found that yeast strains compromised for stages downstream of deadenylation in the major mRNA decay pathway are incapable of inhibiting global translation initiation in response to stress. In the past, the paradigm of the eIF2{alpha} kinase-dependent amino acid starvation pathway in yeast has been used to evaluate this highly conserved stress response in all eukaryotic cells. Using a similar approach we have found that even though the mRNA decay mutants maintain high levels of general translation, they exhibit many of the hallmarks of amino acid starvation, including increased eIF2{alpha} phosphorylation and activated GCN4 mRNA translation. Therefore, these mutants appear translationally oblivious to decreased ternary complex abundance, and we propose that this is due to higher rates of mRNA recruitment to the 40S ribosomal subunit.

* Corresponding author. Mailing address: Department of Biomolecular Sciences, UMIST, Sackville St., P.O. Box 88, Manchester M60 1QD, United Kingdom. Phone: 44 161 200 4164. Fax: 44 161 200 0409. E-mail: mark.p.ashe{at}umist.ac.uk.

Molecular and Cellular Biology, April 2004, p. 2998-3010, Vol. 24, No. 7
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.7.2998-3010.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • di Penta, A., Mercaldo, V., Florenzano, F., Munck, S., Ciotti, M. T., Zalfa, F., Mercanti, D., Molinari, M., Bagni, C., Achsel, T. (2009). Dendritic LSm1/CBP80-mRNPs mark the early steps of transport commitment and translational control. JCB 184: 423-435 [Abstract] [Full Text]  
  • Buchan, J. R., Muhlrad, D., Parker, R. (2008). P bodies promote stress granule assembly in Saccharomyces cerevisiae. JCB 183: 441-455 [Abstract] [Full Text]  
  • Ling, S. H. M., Decker, C. J., Walsh, M. A., She, M., Parker, R., Song, H. (2008). Crystal Structure of Human Edc3 and Its Functional Implications. Mol. Cell. Biol. 28: 5965-5976 [Abstract] [Full Text]  
  • Mascarenhas, C., Edwards-Ingram, L. C., Zeef, L., Shenton, D., Ashe, M. P., Grant, C. M. (2008). Gcn4 Is Required for the Response to Peroxide Stress in the Yeast Saccharomyces cerevisiae. Mol. Biol. Cell 19: 2995-3007 [Abstract] [Full Text]  
  • Beckham, C., Hilliker, A., Cziko, A.-M., Noueiry, A., Ramaswami, M., Parker, R. (2008). The DEAD-Box RNA Helicase Ded1p Affects and Accumulates in Saccharomyces cerevisiae P-Bodies. Mol. Biol. Cell 19: 984-993 [Abstract] [Full Text]  
  • Pilkington, G. R., Parker, R. (2008). Pat1 Contains Distinct Functional Domains That Promote P-Body Assembly and Activation of Decapping. Mol. Cell. Biol. 28: 1298-1312 [Abstract] [Full Text]  
  • Decker, C. J., Teixeira, D., Parker, R. (2007). Edc3p and a glutamine/asparagine-rich domain of Lsm4p function in processing body assembly in Saccharomyces cerevisiae. JCB 179: 437-449 [Abstract] [Full Text]  
  • Yamasaki, S., Stoecklin, G., Kedersha, N., Simarro, M., Anderson, P. (2007). T-cell Intracellular Antigen-1 (TIA-1)-induced Translational Silencing Promotes the Decay of Selected mRNAs. J. Biol. Chem. 282: 30070-30077 [Abstract] [Full Text]  
  • Hoyle, N. P., Castelli, L. M., Campbell, S. G., Holmes, L. E.A., Ashe, M. P. (2007). Stress-dependent relocalization of translationally primed mRNPs to cytoplasmic granules that are kinetically and spatially distinct from P-bodies. JCB 179: 65-74 [Abstract] [Full Text]  
  • Gilbert, W. V., Zhou, K., Butler, T. K., Doudna, J. A. (2007). Cap-Independent Translation Is Required for Starvation-Induced Differentiation in Yeast. Science 317: 1224-1227 [Abstract] [Full Text]  
  • Brengues, M., Parker, R. (2007). Accumulation of Polyadenylated mRNA, Pab1p, eIF4E, and eIF4G with P-Bodies in Saccharomyces cerevisiae. Mol. Biol. Cell 18: 2592-2602 [Abstract] [Full Text]  
  • Whitney, M. L., Hurto, R. L., Shaheen, H. H., Hopper, A. K. (2007). Rapid and Reversible Nuclear Accumulation of Cytoplasmic tRNA in Response to Nutrient Availability. Mol. Biol. Cell 18: 2678-2686 [Abstract] [Full Text]  
  • Teixeira, D., Parker, R. (2007). Analysis of P-Body Assembly in Saccharomyces cerevisiae. Mol. Biol. Cell 18: 2274-2287 [Abstract] [Full Text]  
  • Shenton, D., Smirnova, J. B., Selley, J. N., Carroll, K., Hubbard, S. J., Pavitt, G. D., Ashe, M. P., Grant, C. M. (2006). Global Translational Responses to Oxidative Stress Impact upon Multiple Levels of Protein Synthesis. J. Biol. Chem. 281: 29011-29021 [Abstract] [Full Text]  
  • Segal, S. P., Dunckley, T., Parker, R. (2006). Sbp1p Affects Translational Repression and Decapping in Saccharomyces cerevisiae.. Mol. Cell. Biol. 26: 5120-5130 [Abstract] [Full Text]  
  • Valencia-Sanchez, M. A., Liu, J., Hannon, G. J., Parker, R. (2006). Control of translation and mRNA degradation by miRNAs and siRNAs.. Genes Dev. 20: 515-524 [Abstract] [Full Text]  
  • Swaminathan, S., Masek, T., Molin, C., Pospisek, M., Sunnerhagen, P. (2006). Rck2 Is Required for Reprogramming of Ribosomes during Oxidative Stress. Mol. Biol. Cell 17: 1472-1482 [Abstract] [Full Text]  
  • Smirnova, J. B., Selley, J. N., Sanchez-Cabo, F., Carroll, K., Eddy, A. A., McCarthy, J. E. G., Hubbard, S. J., Pavitt, G. D., Grant, C. M., Ashe, M. P. (2005). Global Gene Expression Profiling Reveals Widespread yet Distinctive Translational Responses to Different Eukaryotic Translation Initiation Factor 2B-Targeting Stress Pathways. Mol. Cell. Biol. 25: 9340-9349 [Abstract] [Full Text]  
  • Campbell, S. G., Hoyle, N. P., Ashe, M. P. (2005). Dynamic cycling of eIF2 through a large eIF2B-containing cytoplasmic body: implications for translation control. JCB 170: 925-934 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»