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J. Biol. Chem., Vol. 281, Issue 39, 28687-28698, September 29, 2006

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Cytoplasmic CstF-77 Protein Belongs to a Masking Complex with Cytoplasmic Polyadenylation Element-binding Protein in Xenopus Oocytes^*

From the Centre de Recherches de Biochimie Macromoléculaire, CNRS, 1919 Route de Mende, 34293 Montpellier Cedex 05, France

Regulated mRNA translation is a hallmark of oocytes and early embryos, of which cytoplasmic polyadenylation is a major mechanism. This process involves multiple protein components, including the CPSF (cleavage and polyadenylation specificity factor), which is also required for nuclear polyadenylation. The CstF (cleavage stimulatory factor), with CPSF, is required for the pre-mRNA cleavage before nuclear polyadenylation. However, some evidence suggests that the CstF-77 subunit might have a function independent of nuclear polyadenylation, which could be related to the cell cycle. As such, we addressed the question whether CstF-77 might have a role in cytoplasmic polyadenylation. We investigated the function of the CstF-77 protein in Xenopus oocytes, and show that CstF-77 has indeed a role in the cytoplasm. The Xenopus CstF-77 protein (X77K) localizes mainly to the nucleus, but also in punctuate cytoplasmic foci. We show that X77K resides in a cytoplasmic complex with eIF4E, CPEB (cytoplasmic polyadenylation element-binding protein), CPSF-100 and XGLD2, but is not required for cytoplasmic polyadenylation per se. Impairment of X77K function in ovo leads to an acceleration of the G₂/M transition, with a premature synthesis of Mos and AuroraA proteins. However, the kinetic of Mos mRNA polyadenylation is not modified. Furthermore, X77K represses mRNA translation in vitro. These results suggest that X77K could be involved in masking of mRNA prior to polyadenylation.

Received for publication, February 6, 2006 , and in revised form, July 27, 2006.

^* This work was supported in part by the Centre National de la Recherche Scientifique and the Association pour la Recherche sur le Cancer (contract numbers 4469 and 3147, to E. M.). 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. S1 and S2.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AM071387 [GenBank] .

¹ Supported by the Ministèredel'éducation nationale, de la Recherche et de l'enseignement supérieur and the Association pour la Recherche sur le Cancer.

² To whom correspondence should be addressed: CRBM, CNRS, 1919 route de Mende, 34293 Montpellier cedex 05, France. Tel.: 33-4-67-61-33-39; Fax: 33-4-67-52-15-59; E-mail: elisabeth.mandart{at}crbm.cnrs.fr.

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