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XB-ART-38828
Biochem Biophys Res Commun December 12, 2008; 377 (2): 653-657.

ElrA and AUF1 differentially bind cyclin B2 mRNA.

Guo X , Gourronc F , Audic Y , Lyons-Levy G , Mitchell T , Hartley RS .


Abstract
In Xenopus embryos, maternal cyclins drive the first 12 cell divisions after which several cyclins are terminally degraded, including cyclin B2. Cyclin B2 disappearance is due to transcription-mediated mRNA deadenylation at the midblastula transition, when transcription initiates and the cell cycle lengthens. To further define the mechanism, we characterized proteins capable of binding cyclin B2 3''UTR. We show that ElrA and AUF1 compete for binding to regions containing cytoplasmic polyadenylation elements (CPEs), with AUF1 binding increasing at the midblastula transition. Deletion of both CPEs abrogates polyadenylation but has no effect on deadenylation or binding of ElrA or AUF1. Overexpression of ElrA or AUF1 does not alter cyclin B2 mRNA stability. These results show that ElrA and AUF1 bind to cyclin B2 mRNA independent of CPEs and function by binding other elements.

PubMed ID: 18930026
PMC ID: PMC2613769
Article link: Biochem Biophys Res Commun
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: ccnb2 elavl1

References [+] :
Aoki, Xenopus cold-inducible RNA-binding protein 2 interacts with ElrA, the Xenopus homolog of HuR, and inhibits deadenylation of specific mRNAs. 2003, Pubmed, Xenbase