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Mol Cell. 2012 Jul 27;47(2):267-80. doi: 10.1016/j.molcel.2012.05.005. Epub 2012 Jun 7.

Rrp6p controls mRNA poly(A) tail length and its decoration with poly(A) binding proteins.

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  • 1Centre for mRNP Biogenesis and Metabolism, Department of Molecular Biology and Genetics, Aarhus University, C.F. Møllers Alle 3, Building 1130, DK-8000 Aarhus C., Denmark.

Abstract

Poly(A) (pA) tail binding proteins (PABPs) control mRNA polyadenylation, stability, and translation. In a purified system, S. cerevisiae PABPs, Pab1p and Nab2p, are individually sufficient to provide normal pA tail length. However, it is unknown how this occurs in more complex environments. Here we find that the nuclear exosome subunit Rrp6p counteracts the in vitro and in vivo extension of mature pA tails by the noncanonical pA polymerase Trf4p. Moreover, PABP loading onto nascent pA tails is controlled by Rrp6p; while Pab1p is the major PABP, Nab2p only associates in the absence of Rrp6p. This is because Rrp6p can interact with Nab2p and displace it from pA tails, potentially leading to RNA turnover, as evidenced for certain pre-mRNAs. We suggest that a nuclear mRNP surveillance step involves targeting of Rrp6p by Nab2p-bound pA-tailed RNPs and that pre-mRNA abundance is regulated at this level.

Copyright © 2012 Elsevier Inc. All rights reserved.

PMID:
22683267
[PubMed - indexed for MEDLINE]
PMCID:
PMC3408791
Free PMC Article
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