Nucleic Acids Research Advance Access originally published online on February 26, 2008
Nucleic Acids Research 2008 36(7):2418-2433; doi:10.1093/nar/gkn080
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Nucleic Acids Research, 2008, Vol. 36, No. 7 2418-2433
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Molecular Biology |
Molecular dissection of mRNA poly(A) tail length control in yeast
Université Victor Segalen Bordeaux 2, CNRS, Institut de Biochimie et Génétique Cellulaires, Bordeaux, France
*To whom correspondence should be addressed. Tel: +33 5 56 99 90 08; Fax: +33 5 56 99 90 08; Email: lionel.minvielle{at}ibgc.cnrs.fr
Received January 30, 2007. Revised February 7, 2008. Accepted February 8, 2008.
In eukaryotic cells, newly synthesized mRNAs acquire a poly(A) tail that plays several fundamental roles in export, translation and mRNA decay. In mammals, PABPN1 controls the processivity of polyadenylation and the length of poly(A) tails during de novo synthesis. This regulation is less well-detailed in yeast. We have recently demonstrated that Nab2p is necessary and sufficient for the regulation of polyadenylation and that the Pab1p/PAN complex may act at a later stage in mRNA metabolism. Here, we show that the presence of both Pab1p and Nab2p in reconstituted pre-mRNA 3'-end processing reactions has no stimulating nor inhibitory effect on poly(A) tail regulation. Importantly, the poly(A)-binding proteins are essential to protect the mature mRNA from being subjected to a second round of processing. We have determined which domains of Nab2p are important to control polyadenylation and found that the RGG-box work in conjunction with the two last essential CCCH-type zinc finger domains. Finally, we have tried to delineate the mechanism by which Nab2p performs its regulation function during polyadenylation: it likely forms a complex with poly(A) tails different from a simple linear deposit of proteins as it has been observed with Pab1p.
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