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

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

研究成果: Article

40 引用 (Scopus)

抄録

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.

元の言語English
ページ(範囲)1111-1123
ページ数13
ジャーナルRNA
4
発行部数9
DOI
出版物ステータスPublished - 01-09-1998

Fingerprint

Alternative Splicing
Glycine
Proteins
hnRNP A1
RNA Recognition Motif
RNA

All Science Journal Classification (ASJC) codes

  • Molecular Biology

これを引用

Maeda, Akira ; Munroe, Stephen H. ; Xu, Rui Ming ; Krainer, Adrian R. / Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1. :: RNA. 1998 ; 巻 4, 番号 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.

:: RNA, 巻 4, 番号 9, 01.09.1998, p. 1111-1123.

研究成果: Article

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

VL - 4

SP - 1111

EP - 1123

JO - RNA

JF - RNA

SN - 1355-8382

IS - 9

ER -