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Molecular and Cellular Biology, September 2007, p. 6469-6483, Vol. 27, No. 18
0270-7306/07/$08.00+0     doi:10.1128/MCB.00332-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

LINE-1 ORF1 Protein Localizes in Stress Granules with Other RNA-Binding Proteins, Including Components of RNA Interference RNA-Induced Silencing Complex{triangledown} ,{dagger}

John L. Goodier,* Lili Zhang, Melissa R. Vetter,{ddagger} and Haig H. Kazazian Jr.

Department of Genetics, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania

Received 23 February 2007/ Returned for modification 12 April 2007/ Accepted 30 May 2007

LINE-1 retrotransposons constitute one-fifth of human DNA and have helped shape our genome. A full-length L1 encodes a 40-kDa RNA-binding protein (ORF1p) and a 150-kDa protein (ORF2p) with endonuclease and reverse transcriptase activities. ORF1p is distinctive in forming large cytoplasmic foci, which we identified as cytoplasmic stress granules. A phylogenetically conserved central region of the protein is critical for wild-type localization and retrotransposition. Yeast two-hybrid screens revealed several RNA-binding proteins that coimmunoprecipitate with ORF1p and colocalize with ORF1p in foci. Two of these proteins, YB-1 and hnRNPA1, were previously reported in stress granules. We identified additional proteins associated with stress granules, including DNA-binding protein A, 9G8, and plasminogen activator inhibitor RNA-binding protein 1 (PAI-RBP1). PAI-RBP1 is a homolog of VIG, a part of the Drosophila melanogaster RNA-induced silencing complex (RISC). Other RISC components, including Ago2 and FMRP, also colocalize with PAI-RBP1 and ORF1p. We suggest that targeting ORF1p, and possibly the L1 RNP, to stress granules is a mechanism for controlling retrotransposition and its associated genetic and cellular damage.

* Corresponding author. Mailing address: Dept. of Genetics, University of Pennsylvania School of Medicine, Rm. 515 CRB, 415 Curie Blvd., Philadelphia, PA 19104. Phone: (215) 898-2080. Fax: (215) 573-7760. E-mail: jgoodier{at}mail.med.upenn.edu

{triangledown} Published ahead of print on 11 June 2007.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} Present address: School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA.

Molecular and Cellular Biology, September 2007, p. 6469-6483, Vol. 27, No. 18
0270-7306/07/$08.00+0     doi:10.1128/MCB.00332-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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