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AU‐rich RNA‐binding induces changes in the quaternary structure of AUH
Author(s) -
Kurimoto Kazuki,
Kuwasako Kanako,
Sandercock Alan M.,
Unzai Satoru,
Robinson Carol V.,
Muto Yutaka,
Yokoyama Shigeyuki
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22246
Subject(s) - trimer , rna , dimer , protein quaternary structure , chemistry , binding site , biochemistry , stereochemistry , microbiology and biotechnology , biophysics , biology , protein subunit , gene , organic chemistry
The human AU RNA binding protein/enoyl‐Coenzyme A hydratase (AUH) is a 3‐hydroxy‐3‐methylglutaconyl‐CoA dehydratase in the leucine degradation pathway. It also possesses an RNA‐binding activity to AUUU repeats, which involves no known conserved RNA‐binding domains and is seemingly unrelated to the enzymatic activity. In this study, we performed mass spectrometric analyses to elucidate the oligomeric states of AUH in the presence and absence of RNA. With a short RNA (AUUU) or without RNA, AUH mainly exists as a trimer in solution. On the other hand, the AUH trimer dimerizes upon binding to one molecule of a long RNA containing 24 repeats of the AUUU motif, (AUUU) 24 A. AUH was crystallized with the long RNA. Although the RNA was disordered in the crystalline lattice, the AUH structure was determined as an asymmetric dimer of trimers with a kink in the alignment of the trimer axes, resulting in the formation of two clefts with significantly different sizes. Proteins 2009. © 2008 Wiley‐Liss, Inc.