UMMS Affiliation

Department of Molecular Genetics and Microbiology

Publication Date

10-29-1997

Document Type

Article

Subjects

Animals; Cytoplasm; Gastrula; Mutation; Poly A; Protein Binding; RNA Processing, Post-Transcriptional; RNA, Messenger; RNA-Binding Proteins; Regulatory Sequences, Nucleic Acid; Sequence Deletion; Transcription Factors; *Xenopus Proteins; Xenopus laevis; *mRNA Cleavage and Polyadenylation Factors

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The translational activation of several maternal mRNAs in Xenopus laevis is dependent on cytoplasmic poly(A) elongation. Messages harboring the UUUUUAU-type cytoplasmic polyadenylation element (CPE) in their 3' untranslated regions (UTRs) undergo polyadenylation and translation during oocyte maturation. This CPE is bound by the protein CPEB, which is essential for polyadenylation. mRNAs that have the poly(U)12-27 embryonic-type CPE (eCPE) in their 3' UTRs undergo polyadenylation and translation during the early cleavage and blastula stages. A 36-kDa eCPE-binding protein in oocytes and embryos has been identified by UV cross-linking. We now report that this 36-kDa protein is ElrA, a member of the ELAV family of RNA-binding proteins. The proteins are identical in size, antibody directed against ElrA immunoprecipitates the 36-kDa protein, and the two proteins have the same RNA binding specificity in vitro. C12 and activin receptor mRNAs, both of which contain eCPEs, are detected in immunoprecipitated ElrA-mRNP complexes from eggs and embryos. In addition, this in vivo interaction requires the eCPE. Although a number of experiments failed to define a role for ElrA in cytoplasmic polyadenylation, the expression of a dominant negative ElrA protein in embryos results in an exogastrulation phenotype. The possible functions of ElrA in gastrulation are discussed.

Rights and Permissions

Citation: Mol Cell Biol. 1997 Nov;17(11):6402-9.

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Molecular and cellular biology

PubMed ID

9343402

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