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ALYREF links 3′‐end processing to nuclear export of non‐polyadenylated mRNA s
Author(s) -
Fan Jing,
Wang Ke,
Du Xian,
Wang Jianshu,
Chen Suli,
Wang Yimin,
Shi Min,
Zhang Li,
Wu Xudong,
Zheng Dinghai,
Wang Changshou,
Wang Lantian,
Tian Bin,
Li Guohui,
Zhou Yu,
Cheng Hong
Publication year - 2019
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.201899910
Subject(s) - biology , polyadenylation , messenger rna , microbiology and biotechnology , biochemistry , gene
The RNA ‐binding protein ALYREF plays key roles in nuclear export and also 3′‐end processing of polyadenylated mRNA s, but whether such regulation also extends to non‐polyadenylated RNA s is unknown. Replication‐dependent ( RD )‐histone mRNA s are not polyadenylated, but instead end in a stem‐loop ( SL ) structure. Here, we demonstrate that ALYREF prevalently binds a region next to the SL on RD ‐histone mRNA s. SL ‐binding protein ( SLBP ) directly interacts with ALYREF and promotes its recruitment. ALYREF promotes histone pre‐ mRNA 3′‐end processing by facilitating U7‐sn RNP recruitment through physical interaction with the U7‐sn RNP ‐specific component Lsm11. Furthermore, ALYREF , together with other components of the TREX complex, enhances histone mRNA export. Moreover, we show that 3′‐end processing promotes ALYREF recruitment and histone mRNA export. Together, our results point to an important role of ALYREF in coordinating 3′‐end processing and nuclear export of non‐polyadenylated mRNA s.