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Molecular and Cellular Biology, February 2008, p. 1298-1312, Vol. 28, No. 4
0270-7306/08/$08.00+0 doi:10.1128/MCB.00936-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Pat1 Contains Distinct Functional Domains That Promote P-Body Assembly and Activation of Decapping
Guy R. Pilkington and
Roy Parker*
Department of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, Tucson, Arizona 85721-0106
Received 25 May 2007/
Returned for modification 6 July 2007/
Accepted 25 October 2007
The control of mRNA degradation and translation are important aspects of gene regulation. Recent results suggest that translation repression and mRNA decapping can be intertwined and involve the formation of a quiescent mRNP, which can accumulate in cytoplasmic foci referred to as P bodies. The Pat1 protein is a key component of this complex and an important activator of decapping, yet little is known about its function. In this work, we analyze Pat1 in Saccharomyces cerevisiae function by deletion and functional analyses. Our results identify two primary functional domains in Pat1: one promoting translation repression and P-body assembly and a second domain promoting mRNA decapping after assembly of the mRNA into a P-body mRNP. In addition, we provide evidence that Pat1 binds RNA and has numerous domain-specific interactions with mRNA decapping factors. These results indicate that Pat1 is an RNA binding protein and a multidomain protein that functions at multiple stages in the process of translation repression and mRNA decapping.
* Corresponding author. Mailing address: Department of Molecular and Cellular Biology and Howard Hughes Medical Institute, University of Arizona, 1007 E. Lowell St., Tucson, AZ 85721-0206. Phone: (520) 621-9347. Fax: (520) 621-4524. E-mail:
rrparker{at}u.arizona.edu
Published ahead of print on 17 December 2007.
Molecular and Cellular Biology, February 2008, p. 1298-1312, Vol. 28, No. 4
0270-7306/08/$08.00+0 doi:10.1128/MCB.00936-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
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