HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 282, Issue 47, 34031-34038, November 23, 2007

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: 282/47/34031    most recent M706363200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nelson, M. R. Articles by Smibert, C. A. Search for Related Content PubMed PubMed Citation Articles by Nelson, M. R. Articles by Smibert, C. A. Social Bookmarking                      What's this?

A Multiprotein Complex That Mediates Translational Enhancement in Drosophila^*

Meryl R. Nelson¹, Hua Luo, Heli K. Vari, Brian J. Cox^¶, Andrew J. Simmonds^||, Henry M. Krause^¶**, Howard D. Lipshitz^¶2, and Craig A. Smibert³

From the Departments of Biochemistry and ^¶Molecular and Medical Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada, the Program in Developmental and Stem Cell Biology, Research Institute, Hospital for Sick Children, Toronto, Ontario M5G 1L7, Canada, the ^**Banting and Best Department of Medical Research, Donnelly Centre for Cellular and Biomolecular Research, Ontario M5S 3E1, Canada, and the ^||Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Modulating the efficiency of translation plays an important role in a wide variety of cellular processes and is often mediated by trans-acting factors that interact with cis-acting sequences within the mRNA. Here we show that a cis-acting element, the Hsp83 degradation element (HDE), within the 3'-untranslated region of the Drosophila Hsp83 mRNA functions as a translational enhancer. We show that this element is bound by a multiprotein complex, and we identify components using a novel affinity-based method called tandem RNA affinity purification tagging. Three proteins (DDP1, Hrp48, and poly(A)-binding protein) are components of the HDE-binding complex and function in translational enhancement. Our data support a model whereby the HDE is composed of several cis-acting subelements that represent binding sites for trans-acting factors, and the combined action of these trans-acting factors underlies the ability of the HDE to stimulate translation.

Received for publication, August 1, 2007 , and in revised form, September 20, 2007.

^* This work was supported in part by an operating grant from the National Cancer Institute of Canada with funds from the Terry Fox Run (to C. A. S.), an operating grant from the Canadian Institutes of Health Research as well as funds from the CRC Program (to H. D. L.), and an operating grant from the National Cancer Institute of Canada with funds from the Canadian Cancer Society (to H. M. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. 1–3.

¹ Supported by an Ontario Graduate Scholarship.

² Canada Research Chair in Developmental Biology. To whom correspondence may be addressed: 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada. Tel.: 416-946-5296; Fax: 416-813-7956; E-mail: howard.lipshitz{at}utoronto.ca.

³ To whom correspondence may be addressed: 1 King's College Circle, Toronto, Ontario M5S 1A8, Canada. Tel.: 416-946-5538; Fax: 416-978-8548; E-mail: c.smibert{at}utoronto.ca.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. L. Semotok, H. Luo, R. L. Cooperstock, A. Karaiskakis, H. K. Vari, C. A. Smibert, and H. D. Lipshitz Drosophila Maternal Hsp83 mRNA Destabilization Is Directed by Multiple SMAUG Recognition Elements in the Open Reading Frame Mol. Cell. Biol., November 15, 2008; 28(22): 6757 - 6772. [Abstract] [Full Text] [PDF]

				R. A. Jain and E. R. Gavis The Drosophila hnRNP M homolog Rumpelstiltskin regulates nanos mRNA localization Development, March 1, 2008; 135(5): 973 - 982. [Abstract] [Full Text] [PDF]