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'Black sheep' that don't leave the double-stranded RNA-binding domain fold.

ABSTRACT: The canonical double-stranded RNA (dsRNA)-binding domain (dsRBD) is composed of an ?1-?1-?2-?3-?2 secondary structure that folds in three dimensions to recognize dsRNA. Recently, structural and functional studies of divergent dsRBDs revealed adaptations that include intra- and/or intermolecular protein interactions, sometimes in the absence of detectable dsRNA-binding ability. We describe here how discrete dsRBD components can accommodate pronounced amino-acid sequence changes while maintaining the core fold. We exemplify the growing importance of divergent dsRBDs in mRNA decay by discussing Dicer, Staufen (STAU)1 and 2, trans-activation responsive RNA-binding protein (TARBP)2, protein activator of protein kinase RNA-activated (PKR) (PACT), DiGeorge syndrome critical region (DGCR)8, DEAH box helicase proteins (DHX) 9 and 30, and dsRBD-like fold-containing proteins that have ribosome-related functions. We also elaborate on the computational limitations to discovering yet-to-be-identified divergent dsRBDs.

SUBMITTER: Gleghorn ML

PROVIDER: S-EPMC4077987 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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'Black sheep' that don't leave the double-stranded RNA-binding domain fold.

Gleghorn Michael L ML Maquat Lynne E LE

Trends in biochemical sciences 20140619 7

The canonical double-stranded RNA (dsRNA)-binding domain (dsRBD) is composed of an α1-β1-β2-β3-α2 secondary structure that folds in three dimensions to recognize dsRNA. Recently, structural and functional studies of divergent dsRBDs revealed adaptations that include intra- and/or intermolecular protein interactions, sometimes in the absence of detectable dsRNA-binding ability. We describe here how discrete dsRBD components can accommodate pronounced amino-acid sequence changes while maintaining ...[more]

PMID: 24954387

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