Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 1, Pages 127-U161Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2468
Keywords
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Funding
- US National Institute of Environmental Health Science [ES06694]
- US National Institutes of Health
- US National Cancer Institute [CA023074]
- BIO5 Institute of the University of Arizona
- US National Center for Research Resources [1S10 RR028868-01]
- US National Institutes of Health [7R37 GM045443]
- Howard Hughes Medical Institute
- Leukemia and Lymphoma Society [5687-13]
- NATIONAL CANCER INSTITUTE [P30CA023074] Funding Source: NIH RePORTER
- NATIONAL CENTER FOR RESEARCH RESOURCES [S10RR028868] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES [P30ES006694] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM045443] Funding Source: NIH RePORTER
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Proteins regulate gene expression by controlling mRNA biogenesis, localization, translation and decay. Identifying the composition, diversity and function of mRNA-protein complexes (mRNPs) is essential to understanding these processes. In a global survey of Saccharomyces cerevisiae mRNA-binding proteins, we identified 120 proteins that cross-link to mRNA, including 66 new mRNA-binding proteins. These include kinases, RNA-modification enzymes, metabolic enzymes and tRNA-and rRNA-metabolism factors. These proteins show dynamic subcellular localization during stress, including assembly into stress granules and processing bodies (P bodies). Cross-linking and immunoprecipitation (CLIP) analyses of the P-body components Pat1, Lsm1, Dhh1 and Sbp1 identified sites of interaction on specific mRNAs, revealing positional binding preferences and co-assembly preferences. When taken together, this work defines the major yeast mRNP proteins, reveals widespread changes in their subcellular location during stress and begins to define assembly rules for P-body mRNPs.
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