ALYREF links 3′-end processing to nuclear export of non-polyadenylated mRNAs

Jing Fan, Ke Wang, Xian Du, Jianshu Wang, Suli Chen, Yimin Wang, Min Shi, Li Zhang, Xudong Wu, Dinghai Zheng, Changshou Wang, Lantian Wang, Bin Tian, Guohui Li, Yu Zhou, Hong Cheng

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Article numbere99910
JournalEMBO Journal
Volume38
Issue number9
DOIs
StatePublished - May 2 2019
Externally publishedYes

Fingerprint

Cell Nucleus Active Transport
Histones
U7 Small Nuclear Ribonucleoproteins
Messenger RNA
Processing
RNA-Binding Proteins
RNA Precursors
Carrier Proteins
RNA

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

Keywords

  • 3′-end processing
  • ALYREF
  • mRNA export
  • RD-histone mRNA
  • SLBP

Cite this

Fan, J., Wang, K., Du, X., Wang, J., Chen, S., Wang, Y., ... Cheng, H. (2019). ALYREF links 3′-end processing to nuclear export of non-polyadenylated mRNAs. EMBO Journal, 38(9), [e99910]. https://doi.org/10.15252/embj.201899910
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. / ALYREF links 3′-end processing to nuclear export of non-polyadenylated mRNAs. In: EMBO Journal. 2019 ; Vol. 38, No. 9.
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abstract = "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.",
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Fan, J, Wang, K, Du, X, Wang, J, Chen, S, Wang, Y, Shi, M, Zhang, L, Wu, X, Zheng, D, Wang, C, Wang, L, Tian, B, Li, G, Zhou, Y & Cheng, H 2019, 'ALYREF links 3′-end processing to nuclear export of non-polyadenylated mRNAs', EMBO Journal, vol. 38, no. 9, e99910. https://doi.org/10.15252/embj.201899910

ALYREF links 3′-end processing to nuclear export of non-polyadenylated mRNAs. / 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.

In: EMBO Journal, Vol. 38, No. 9, e99910, 02.05.2019.

Research output: Contribution to journalArticle

TY - JOUR

T1 - ALYREF links 3′-end processing to nuclear export of non-polyadenylated mRNAs

AU - Fan, Jing

AU - Wang, Ke

AU - Du, Xian

AU - Wang, Jianshu

AU - Chen, Suli

AU - Wang, Yimin

AU - Shi, Min

AU - Zhang, Li

AU - Wu, Xudong

AU - Zheng, Dinghai

AU - Wang, Changshou

AU - Wang, Lantian

AU - Tian, Bin

AU - Li, Guohui

AU - Zhou, Yu

AU - Cheng, Hong

PY - 2019/5/2

Y1 - 2019/5/2

N2 - 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.

AB - 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.

KW - 3′-end processing

KW - ALYREF

KW - mRNA export

KW - RD-histone mRNA

KW - SLBP

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