Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1

Akira Maeda, Stephen H. Munroe, Rui Ming Xu, Adrian R. Krainer

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

hnRNP A1 regulates alternative splicing by antagonizing SR proteins. It consists of two closely related, tandem RNA-recognition motifs (RRMs), followed by a glycine-rich domain. Analysis of variant proteins with duplications, deletions, or swaps of the RRMs showed that although both RRMs are required for alternative splicing function, each RRM plays distinct roles, and their relative position is important. Surprisingly, RRM2 but not RRM1 could support this function when duplicated, despite their very similar structure. Specific RNA binding and annealing are not sufficient for hnRNP A1 alternative splicing function. These observations, together with phylogenetic and structural data, suggest that the two RRMs are quasi-symmetric but functionally nonequivalent modules that evolved as components of a single bipartite domain.

Original languageEnglish
Pages (from-to)1111-1123
Number of pages13
JournalRNA
Volume4
Issue number9
DOIs
Publication statusPublished - 01-09-1998

Fingerprint

Alternative Splicing
Glycine
Proteins
hnRNP A1
RNA Recognition Motif
RNA

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

Maeda, Akira ; Munroe, Stephen H. ; Xu, Rui Ming ; Krainer, Adrian R. / Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1. In: RNA. 1998 ; Vol. 4, No. 9. pp. 1111-1123.
@article{da6a05fa21c643dba5028c79372e636a,
title = "Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1",
abstract = "hnRNP A1 regulates alternative splicing by antagonizing SR proteins. It consists of two closely related, tandem RNA-recognition motifs (RRMs), followed by a glycine-rich domain. Analysis of variant proteins with duplications, deletions, or swaps of the RRMs showed that although both RRMs are required for alternative splicing function, each RRM plays distinct roles, and their relative position is important. Surprisingly, RRM2 but not RRM1 could support this function when duplicated, despite their very similar structure. Specific RNA binding and annealing are not sufficient for hnRNP A1 alternative splicing function. These observations, together with phylogenetic and structural data, suggest that the two RRMs are quasi-symmetric but functionally nonequivalent modules that evolved as components of a single bipartite domain.",
author = "Akira Maeda and Munroe, {Stephen H.} and Xu, {Rui Ming} and Krainer, {Adrian R.}",
year = "1998",
month = "9",
day = "1",
doi = "10.1017/S135583829898089X",
language = "English",
volume = "4",
pages = "1111--1123",
journal = "RNA",
issn = "1355-8382",
publisher = "Cold Spring Harbor Laboratory Press",
number = "9",

}

Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1. / Maeda, Akira; Munroe, Stephen H.; Xu, Rui Ming; Krainer, Adrian R.

In: RNA, Vol. 4, No. 9, 01.09.1998, p. 1111-1123.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1

AU - Maeda, Akira

AU - Munroe, Stephen H.

AU - Xu, Rui Ming

AU - Krainer, Adrian R.

PY - 1998/9/1

Y1 - 1998/9/1

N2 - hnRNP A1 regulates alternative splicing by antagonizing SR proteins. It consists of two closely related, tandem RNA-recognition motifs (RRMs), followed by a glycine-rich domain. Analysis of variant proteins with duplications, deletions, or swaps of the RRMs showed that although both RRMs are required for alternative splicing function, each RRM plays distinct roles, and their relative position is important. Surprisingly, RRM2 but not RRM1 could support this function when duplicated, despite their very similar structure. Specific RNA binding and annealing are not sufficient for hnRNP A1 alternative splicing function. These observations, together with phylogenetic and structural data, suggest that the two RRMs are quasi-symmetric but functionally nonequivalent modules that evolved as components of a single bipartite domain.

AB - hnRNP A1 regulates alternative splicing by antagonizing SR proteins. It consists of two closely related, tandem RNA-recognition motifs (RRMs), followed by a glycine-rich domain. Analysis of variant proteins with duplications, deletions, or swaps of the RRMs showed that although both RRMs are required for alternative splicing function, each RRM plays distinct roles, and their relative position is important. Surprisingly, RRM2 but not RRM1 could support this function when duplicated, despite their very similar structure. Specific RNA binding and annealing are not sufficient for hnRNP A1 alternative splicing function. These observations, together with phylogenetic and structural data, suggest that the two RRMs are quasi-symmetric but functionally nonequivalent modules that evolved as components of a single bipartite domain.

UR - http://www.scopus.com/inward/record.url?scp=0031690775&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031690775&partnerID=8YFLogxK

U2 - 10.1017/S135583829898089X

DO - 10.1017/S135583829898089X

M3 - Article

C2 - 9740129

AN - SCOPUS:0031690775

VL - 4

SP - 1111

EP - 1123

JO - RNA

JF - RNA

SN - 1355-8382

IS - 9

ER -