Unwinding by Local Strand Separation Is Critical for the Function of DEAD-Box Proteins as RNA Chaperones
- 19 June 2009
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 389 (4), 674-693
- https://doi.org/10.1016/j.jmb.2009.04.043
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (F32 GM076961, GM037951, GM067700)
This publication has 60 references indexed in Scilit:
- The ATPase Cycle Mechanism of the DEAD-box rRNA Helicase, DbpAJournal of Molecular Biology, 2008
- Function of the C-terminal Domain of the DEAD-box Protein Mss116p Analyzed in Vivo and in VitroJournal of Molecular Biology, 2008
- Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperoneNature, 2007
- Do DEAD-Box Proteins Promote Group II Intron Splicing without Unwinding RNA?Molecular Cell, 2007
- Probing the Mechanisms of DEAD-Box Proteins as General RNA Chaperones: The C-Terminal Domain of CYT-19 Mediates General Recognition of RNABiochemistry, 2007
- Involvement of DEAD-box Proteins in Group I and Group II Intron Splicing. Biochemical Characterization of Mss116p, ATP Hydrolysis-dependent and -independent Mechanisms, and General RNA Chaperone ActivityJournal of Molecular Biology, 2007
- Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperoneProceedings of the National Academy of Sciences of the United States of America, 2006
- Protein production by auto-induction in high-density shaking culturesProtein Expression and Purification, 2005
- Multifunctional yeast high-copy-number shuttle vectorsGene, 1992
- A positive selection for mutants lacking orotidine-5′-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistanceMolecular Genetics and Genomics, 1984