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GENES & DEVELOPMENT 18:1513-1526, 2004
©2004 by Cold Spring Harbor Laboratory Press; ISSN 0890-9369/ $5.00
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REVIEW

U2AF homology motifs: protein recognition in the RRM world

Clara L. Kielkopf1,3, Stephan Lücke2 and Michael R. Green2,4

1 Department of Biochemistry and Molecular Biology, Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205, USA; 2 Howard Hughes Medical Institute, Programs in Gene Function and Expression and Molecular Medicine, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA

Recent structures of the heterodimeric splicing factor U2 snRNP auxiliary factor (U2AF) have revealed two unexpected examples of RNA recognition motif (RRM)-like domains with specialized features for protein recognition. These unusual RRMs, called U2AF homology motifs (UHMs), represent a novel class of protein recognition motifs. Defining a set of rules to distinguish traditional RRMs from UHMs is key to identifying novel UHM family members. Here we review the critical sequence features necessary to mediate protein–UHM interactions, and perform comprehensive database searches to identify new members of the UHM family. The resulting implications for the functional and evolutionary relationships among candidate UHM family members are discussed.

[Keywords: U2AF; RNA recognition motif; protein–protein interaction; RNA-binding domain; PUMP; splicing factor]


Article and publication are at http://www.genesdev.org/cgi/doi/10.1101/gad.1206204.

Corresponding authors.

3 E-MAIL ckielkop{at}jhsph.edu; FAX (410) 955-2926.

4 E-MAIL michael.green{at}umassmed.edu; FAX (508) 856-5473.


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