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Assembly of an Export-Competent mRNP Is Needed for Efficient Release of the 3′-End Processing Complex after Polyadenylation
被引:55
作者:
Qu, Xiangping
[2
]
Lykke-Andersen, Soren
[1
]
Nasser, Tommy
[1
]
Saguez, Cyril
[1
]
Bertrand, Edouard
[3
]
Jensen, Torben Heick
[1
]
Moore, Claire
[2
]
机构:
[1] Aarhus Univ, Dept Mol Biol, Ctr mRNP Biogenesis & Metab, DK-8000 Aarhus C, Denmark
[2] Tufts Univ, Sch Med, Dept Mol Biol & Microbiol, Boston, MA 02111 USA
[3] CNRS, UMR 5535, Inst Mol Genet Montpellier, F-34293 Montpellier, France
基金:
美国国家卫生研究院;
新加坡国家研究基金会;
关键词:
MESSENGER-RNA EXPORT;
TAIL LENGTH CONTROL;
BOX PROTEIN DBP5;
YEAST POLY(A)-BINDING PROTEIN;
NUCLEAR EXPORT;
SACCHAROMYCES-CEREVISIAE;
BINDING PROTEIN;
COTRANSCRIPTIONAL RECRUITMENT;
TRANSCRIPTIONAL ELONGATION;
MITOTIC RECOMBINATION;
D O I:
10.1128/MCB.00468-09
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Before polyadenylated mRNA is exported from the nucleus, the 3'-end processing complex is removed by a poorly described mechanism. In this study, we asked whether factors involved in mRNP maturation and export are also required for disassembly of the cleavage and polyadenylation complex. An RNA immunoprecipitation assay monitoring the amount of the cleavage factor (CF) IA component Rna15p associated with poly(A)(+) RNA reveals defective removal of Rna15p in mutants of the nuclear export receptor Mex67p as well as other factors important for assembly of an export-competent mRNP. In contrast, Rna15p is not retained in mutants of export factors that function primarily on the cytoplasmic side of the nuclear pore. Consistent with a functional interaction between Mex67p and the 3'-end processing complex, a mex67 mutant accumulates unprocessed SSA4 transcripts and exhibits a severe growth defect when this mutation is combined with mutation of Rna15p or another CF IA subunit, Rna14p. RNAs that become processed in a mex67 mutant have longer poly(A) tails both in vivo and in vitro. This influence of Mex67p on 3'-end processing is conserved, as depletion of its human homolog, TAP/NXF1, triggers mRNA hyperadenylation. Our results indicate a function for nuclear mRNP assembly factors in releasing the 3'-end processing complex once polyadenylation is complete.
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页码:5327 / 5338
页数:12
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