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

Akila Mayeda, 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

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Fingerprint Dive into the research topics of 'Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1'. Together they form a unique fingerprint.

  • Cite this