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Biochem Biophys Res Commun. 2008 Dec 12;377(2):653-657. doi: 10.1016/j.bbrc.2008.10.029. Epub 2008 Oct 16.

ElrA and AUF1 differentially bind cyclin B2 mRNA.

Author information

1
Cell Biology and Physiology, University of New Mexico HSC, MSC08 4750, Albuquerque, NM 87131, USA.
2
Microbiology, University of Iowa Hospitals and Clinics, Iowa City, IA 52242, USA.
3
Laboratoire de Genetique du Developpement CNRS-UMR6061, Universite de Rennes I, CS 34317, 35043 Rennes, France.
4
Cell Biology and Physiology, University of New Mexico HSC, MSC08 4750, Albuquerque, NM 87131, USA. Electronic address: rhartley@salud.unm.edu.

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.

PMID:
18930026
PMCID:
PMC2613769
DOI:
10.1016/j.bbrc.2008.10.029
[Indexed for MEDLINE]
Free PMC Article

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