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In Vitro Deadenylation of Mammalian MRNA by a HeLa Cell 3' Exonuclease

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Journal EMBO J
Date 1991 Oct 1
PMID 1717259
Citations 38
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Abstract

We have identified a 3' exonuclease in HeLa cell extracts which deadenylates mammalian mRNA and leaves the mRNA body intact after poly(A) removal. Only homopolymeric adenosine tails located at the 3' end were efficiently removed by the exonuclease. The poly(A) removing activity did not require any specific sequences in the mRNA body either for poly(A) removal or for accumulation of the deadenylated mRNA. We conclude that the poly(A) removing activity is a 3' exonuclease since (i) reaction intermediates gradually lose the poly(A) tail, (ii) degradation is prevented by the presence of a cordycepin residue at the 3' end and (iii) RNAs having internally located poly(A) stretches are poor substrates for degradation. The possible involvement of the poly(A) removing enzyme in regulating mRNA translation and stability is discussed.

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References
1.
Bernstein P, Peltz S, Ross J . The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro. Mol Cell Biol. 1989; 9(2):659-70. PMC: 362643. DOI: 10.1128/mcb.9.2.659-670.1989. View

2.
McGrew L, Dworkin M, Richter J . Poly(A) elongation during Xenopus oocyte maturation is required for translational recruitment and is mediated by a short sequence element. Genes Dev. 1989; 3(6):803-15. DOI: 10.1101/gad.3.6.803. View

3.
Sachs A, Davis R . The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation. Cell. 1989; 58(5):857-67. DOI: 10.1016/0092-8674(89)90938-0. View

4.
Swartwout S, Kinniburgh A . c-myc RNA degradation in growing and differentiating cells: possible alternate pathways. Mol Cell Biol. 1989; 9(1):288-95. PMC: 362171. DOI: 10.1128/mcb.9.1.288-295.1989. View

5.
Fox C, Sheets M, Wickens M . Poly(A) addition during maturation of frog oocytes: distinct nuclear and cytoplasmic activities and regulation by the sequence UUUUUAU. Genes Dev. 1989; 3(12B):2151-62. DOI: 10.1101/gad.3.12b.2151. View