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Molecular and Cellular Biology, December 2006, p. 8803-8813, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.00090-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Polysome-Bound Endonuclease PMR1 Is Targeted to Stress Granules via Stress-Specific Binding to TIA-1{triangledown}

Feng Yang,1,{dagger} Yong Peng,1,{ddagger} Elizabeth L. Murray,1,{ddagger} Yuichi Otsuka,1 Nancy Kedersha,2 and Daniel R. Schoenberg1*

Department of Molecular and Cellular Biochemistry, The RNA Group and The Comprehensive Cancer Center, The Ohio State University, Columbus, Ohio 43221,1 Division of Rheumatology and Immunology, Brigham and Women's Hospital, Boston, Massachusetts 021152

Received 13 January 2006/ Returned for modification 13 February 2006/ Accepted 1 September 2006

The generalized process of mRNA decay involves deadenylation followed by release from translating polysomes, decapping, and exonuclease decay of the mRNA body. In contrast the mRNA endonuclease PMR1 forms a selective complex with its translating substrate mRNA, where it initiates decay by cleaving within the mRNA body. In stressed cells the phosphorylation of the {alpha} subunit of eukaryotic initiation factor 2 causes translating mRNAs to accumulate with stalled 48S subunits in large subcellular structures termed stress granules (SGs), wherein mRNAs undergo sorting for reinitiation, storage, or decay. Given the unique relationship between translation and PMR1-mediated mRNA decay, we examined the impact of stress-induced dissociation of polysomes on this process. Arsenite stress disrupts the polysome binding of PMR1 and its substrate mRNA but has no impact on the critical tyrosine phosphorylation of PMR1, its association with substrate mRNA, or its association with the functional ~680-kDa mRNP complex in which it normally resides on polysomes. We show that arsenite stress drives PMR1 into an RNase-resistant complex with TIA-1, and we identify a distinct domain in the N terminus of PMR1 that facilitates its interaction with TIA-1. Finally, we show that arsenite promotes the delayed association of PMR1 with SGs under conditions which cause tristetraprolin and butyrate response factor 1, proteins that facilitate exonucleolytic mRNA, to exit SGs.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biochemistry, The Ohio State University, 1645 Neil Ave., Columbus, OH 43210-1218. Phone: (614) 688-3012. Fax: (614) 292-4118. E-mail: schoenberg.3{at}osu.edu.

{triangledown} Published ahead of print on 18 September 2006.

{dagger} Present address: Department of Biology, Johns Hopkins University, Baltimore, Md.

{ddagger} These authors contributed equally to this work.

Molecular and Cellular Biology, December 2006, p. 8803-8813, Vol. 26, No. 23
0270-7306/06/$08.00+0     doi:10.1128/MCB.00090-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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