Xenopus cold-inducible RNA-binding protein 2 interacts with ElrA, the Xenopus homolog of HuR, and inhibits deadenylation of specific mRNAs - PubMed (original) (raw)

. 2003 Nov 28;278(48):48491-7.

doi: 10.1074/jbc.M308328200. Epub 2003 Sep 17.

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Xenopus cold-inducible RNA-binding protein 2 interacts with ElrA, the Xenopus homolog of HuR, and inhibits deadenylation of specific mRNAs

Kazuma Aoki et al. J Biol Chem. 2003.

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Abstract

Xenopus cold-inducible RNA-binding protein 2 (xCIRP2) is a major cytoplasmic RNA-binding protein in oocytes. In this study, we identify another RNA-binding protein ElrA, the Xenopus homolog of HuR, as an interacting protein of xCIRP2 by yeast two-hybrid screening. As ElrA stabilizes the RNA body in the in vitro mRNA stability system, we examine the role of xCIRP2 in the stabilization of mRNA and find that xCIRP2 inhibits deadenylation of AU-rich element-containing mRNA. These results suggest that xCIRP2 and ElrA may be involved in the regulation of mRNA stability at different steps. By immunoprecipitation with anti-xCIRP2 antibody, we find that xCIRP2 interacts with several mRNAs including mRNA encoding the centrosomal kinase Nek2B in oocytes. xCIRP2 also inhibits deadenylation of the mRNA substrate containing the 3'-untranslated region of Nek2B mRNA in the in vitro system. Our results suggest that xCIRP2 associates with specific mRNAs and can regulate the length of poly(A) tail in Xenopus oocytes.

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