Regulation of the Dbp5 ATPase cycle in mRNP remodeling at the nuclear pore: a lively new paradigm for DEAD-box proteins
- Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94143, USA
Abstract
It is commonly assumed that all DEAD-box ATPases function via a shared mechanism, since this is the case for the few proteins characterized thus far. Hodge and colleagues (pp. 1052–1064) and Noble and colleagues (pp. 1065–1077) now describe a novel model for Dbp5's ATPase cycle in mRNA (messenger RNA)/protein complex (mRNP) remodeling during nuclear export. Notably, unlike other DEAD-box proteins, Dbp5 uses a conformational change distinct from ATP hydrolysis for its activity and requires an ADP release factor to reset its ATPase cycle.
Keywords
- nucleocytoplasmic transport
- DEAD-box proteins
- nuclear pore complex
- dominant-negative mutants
- nucleotide exchange factors
- ADP
Footnotes
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↵1 Corresponding author.
E-MAIL christineguthrie{at}gmail.com; FAX (415) 502-5306.
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Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.2062611.
- Copyright © 2011 by Cold Spring Harbor Laboratory Press
