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The Yeast Cytoplasmic LsmI/Pat1p Complex Protects mRNA 3' Termini From Partial Degradation
Weihai Hea and Roy Parkerba Department of Molecular and Cellular Biology, University of Arizona, Tucson, Arizona 85721
b Howard Hughes Medical Institute, University of Arizona, Tucson, Arizona 85721
Corresponding author: Roy Parker, Department of Molecular and Cellular Biology and Howard Hughes Medical Institute, Life Sciences South 404, University of Arizona, Tucson, AZ 85721., rrparker{at}u.arizona.edu (E-mail)
Communicating editor: S. SANDMEYER
strain, wherein the decapping enzyme is lacking. This indicates that trimming is not simply a consequence of the inhibition of mRNA decapping. Third, the temperature-sensitive growth of lsm and pat1 mutants was suppressed by mutations in the exosome or the functionally related Ski proteins, which are required for efficient 3' to 5' mRNA degradation of mRNA. Moreover, in lsm ski double mutants, higher levels of the trimmed mRNAs accumulated, indicating that exosome function is not required for mRNA trimming but that the exosome does degrade the trimmed mRNAs. These results raise the possibility that the temperature-sensitive growth of the lsm1-7 and pat1 mutants is at least partially due to mRNA trimming, which either inactivates the function of the mRNAs or makes them available for premature 3' to 5' degradation by the exosome.
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