Document Detail


RBFOX and SUP-12 sandwich a G base to cooperatively regulate tissue-specific splicing.
MedLine Citation:
PMID:  25132178     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Tissue-specific alternative pre-mRNA splicing is often cooperatively regulated by multiple splicing factors, but the structural basis of cooperative RNA recognition is poorly understood. In Caenorhabditis elegans, ligand binding specificity of fibroblast growth factor receptors (FGFRs) is determined by mutually exclusive alternative splicing of the sole FGFR gene, egl-15. Here we determined the solution structure of a ternary complex of the RNA-recognition motif (RRM) domains from the RBFOX protein ASD-1, SUP-12 and their target RNA from egl-15. The two RRM domains cooperatively interact with the RNA by sandwiching a G base to form the stable complex. Multichromatic fluorescence splicing reporters confirmed the requirement of the G and the juxtaposition of the respective cis elements for effective splicing regulation in vivo. Moreover, we identified a new target for the heterologous complex through an element search, confirming the functional significance of the intermolecular coordination.
Authors:
Kanako Kuwasako; Mari Takahashi; Satoru Unzai; Kengo Tsuda; Seiko Yoshikawa; Fahu He; Naohiro Kobayashi; Peter Güntert; Mikako Shirouzu; Takuhiro Ito; Akiko Tanaka; Shigeyuki Yokoyama; Masatoshi Hagiwara; Hidehito Kuroyanagi; Yutaka Muto
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-8-17
Journal Detail:
Title:  Nature structural & molecular biology     Volume:  -     ISSN:  1545-9985     ISO Abbreviation:  Nat. Struct. Mol. Biol.     Publication Date:  2014 Aug 
Date Detail:
Created Date:  2014-8-18     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101186374     Medline TA:  Nat Struct Mol Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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