ALYREF links 3'-end processing to nuclear export of non-polyadenylated mRNAs.
Active Transport, Cell Nucleus
Exodeoxyribonucleases
/ genetics
Histones
/ genetics
Humans
Nuclear Proteins
/ genetics
Nucleocytoplasmic Transport Proteins
/ genetics
Phosphoproteins
/ genetics
RNA Processing, Post-Transcriptional
RNA Transport
RNA, Messenger
/ genetics
RNA-Binding Proteins
/ genetics
Ribonucleoprotein, U7 Small Nuclear
/ genetics
Transcription Factors
/ genetics
ALYREF
SLBP
3′‐end processing
RD‐histone mRNA
mRNA export
Journal
The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664
Informations de publication
Date de publication:
02 05 2019
02 05 2019
Historique:
received:
05
06
2018
revised:
19
01
2019
accepted:
14
02
2019
pubmed:
13
3
2019
medline:
7
1
2020
entrez:
13
3
2019
Statut:
ppublish
Résumé
The RNA-binding protein ALYREF plays key roles in nuclear export and also 3'-end processing of polyadenylated mRNAs, but whether such regulation also extends to non-polyadenylated RNAs is unknown. Replication-dependent (RD)-histone mRNAs 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 mRNAs. SL-binding protein (SLBP) directly interacts with ALYREF and promotes its recruitment. ALYREF promotes histone pre-mRNA 3'-end processing by facilitating U7-snRNP recruitment through physical interaction with the U7-snRNP-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 mRNAs.
Identifiants
pubmed: 30858280
pii: embj.201899910
doi: 10.15252/embj.201899910
pmc: PMC6484419
pii:
doi:
Substances chimiques
ALYREF protein, human
0
Histones
0
NXF1 protein, human
0
Nuclear Proteins
0
Nucleocytoplasmic Transport Proteins
0
Phosphoproteins
0
RNA, Messenger
0
RNA-Binding Proteins
0
Ribonucleoprotein, U7 Small Nuclear
0
Transcription Factors
0
Exodeoxyribonucleases
EC 3.1.-
three prime repair exonuclease 1
EC 3.1.16.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM084089
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM129069
Pays : United States
Informations de copyright
© 2019 The Authors.
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