Translational Repression by Deadenylases英文文献.pdfVIP

THE JOURNAL OF BIOLOGICAL CHEMISTRY VOL. 285, NO. 37, pp. 28506–28513, September 10, 2010 © 2010 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in the U.S.A. □ Translational Repression by Deadenylases* S Received for publication, June 2, 2010, and in revised form, July 14, 2010 Published, JBC Papers in Press, July 15, 2010, DOI 10.1074/jbc.M110.150763 ‡§ ‡ ‡1 Amy Cooke , Andrew Prigge , and Marvin Wickens From the ‡Department of Biochemistry and the §Cellular and Molecular Biology Program, University of Wisconsin, Madison, Wisconsin 53706 The CCR4-CAF1-NOT complex is a major cytoplasmic dead- for repression, yet in others it is dispensable (5, 6, 37). For exam- enylation complex in yeast and mammals. This complex associ- ple, in budding yeast, CAF1 is required for repression of ates with RNA-binding proteins and microRNAs to repress mRNAs targeted by the regulatory protein, PUF5, even though translation of target mRNAs. We sought to determine deadenylation of the target is not (24). Similarly, miRNA com- how CCR4 and CAF1 participate in repression and control of plexes elicit deadenylation via the CCR4-CAF1 complex, yet maternal mRNAs using Xenopus laevis oocytes. We show that deadenylation is not essential for repression (13, 22, 37–39). Xenopus CCR4 and CAF1 enzymes are active deadenylases These findings suggest that the deadenylase enzymes CCR4 and and repress translation of an adenylated mRNA. CAF1 also