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

Published online by Cambridge University Press:  01 September 1998

AKILA MAYEDA ,
STEPHEN H. MUNROE ,
RUI-MING XU  and
ADRIAN R. KRAINER
AKILA MAYEDA
Affiliation:
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA
STEPHEN H. MUNROE
Affiliation:
Department of Biology, Marquette University, Milwaukee, Wisconsin 53201, USA
RUI-MING XU
Affiliation:
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA
ADRIAN R. KRAINER
Affiliation:
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA
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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.

Keywords

alternative splicinghnRNP A1RNA bindingRNA-recognition motif (RRM)RNA–RNA annealing
Type
Research Article
Information
RNA , Volume 4 , Issue 9 , September 1998 , pp. 1111 - 1123
Copyright
© 1998 RNA Society

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Footnotes

Reprint requests to: Adrian R. Krainer, Cold Spring Harbor Laboratory, P.O. Box 100, 1 Bungtown Road, Cold Spring Harbor, New York 11724-2208, USA; e-mail: krainer@cshl.org. or to Stephen H. Munroe, Department of Biology, Marquette University, P.O. Box 1881, Milwaukee, Wisconsin 53201, USA. e-mail: munroes@vms.csd.mu.edu.