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

Akila Mayeda, Stephen H. Munroe, Rui Ming Xu, Adrian R. Krainer

研究成果: Article

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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

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All Science Journal Classification (ASJC) codes

  • Molecular Biology

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