The m6A-methylase complex recruits TREX and regulates mRNA export

被引：97
|
作者：
Lesbirel, Simon [1 ]
Viphakone, Nicolas [1 ]
Parker, Matthew [1 ]
Parker, Jacob [1 ]
Heath, Catherine [1 ]
Sudbery, Ian [1 ]
Wilson, Stuart A. [1 ]
机构：
[1] Univ Sheffield, Sheffield Inst Nucle Acids SInFoNiA, Dept Mol Biol & Biotechnol, Firth Court Western Bank, Sheffield S10 2TN, S Yorkshire, England
来源：
SCIENTIFIC REPORTS | 2018年 / 8卷
基金：
英国生物技术与生命科学研究理事会;
关键词：
M(6)A RNA; STRUCTURAL BASIS; GENE-EXPRESSION; NUCLEAR EXPORT; METHYLATION; PROTEINS; REVEALS; BINDING; ALYREF; IDENTIFICATION;
D O I：
10.1038/s41598-018-32310-8
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
N-6-methyladenosine (m(6)A) is the most abundant internal modification of eukaryotic mRNA. This modification has previously been shown to alter the export kinetics for mRNAs though the molecular details surrounding this phenomenon remain poorly understood. Recruitment of the TREX mRNA export complex to mRNA is driven by transcription, 5' capping and pre-mRNA splicing. Here we identify a fourth mechanism in human cells driving the association of TREX with mRNA involving the m(6)A methylase complex. We show that the m(6)A complex recruits TREX to m(6)A modified mRNAs and this process is essential for their efficient export. TREX also stimulates recruitment of the m(6)A reader protein YTHDC1 to the mRNA and the m(6)A complex influences the interaction of TREX with YTHDC1. Together our studies reveal a key role for TREX in the export of m(6)A modified mRNAs.
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页数：12
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