Journal
MOLECULAR CELL
Volume 28, Issue 2, Pages 253-263Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2007.08.016
Keywords
-
Categories
Funding
- NIGMS NIH HHS [GM067700, F32-GM76961, R01 GM067700-06, GM037951, R01 GM067700] Funding Source: Medline
Ask authors/readers for more resources
DEAD-box proteins catalyze ATP-driven, local structural changes in RNA or RNA-protein complexes (RNP) during which only few RNA base pairs are separated. It is unclear how duplex unwinding by DEAD-box proteins differs from unwinding by canonical helicases, which can separate many base pairs by directional and processive translocation on the nucleic acid, starting from a helical end. Here, we show that two different DEAD-box proteins, Ded1p and Mss1 16p, can unwind RNA duplexes from internal as well as terminal helical regions and act on RNA segments as small as two nucleotides flanked by DNA. The data indicate that duplex unwinding by DEAD-box proteins is based on local destabilization of RNA helical regions. No directional movement of the enzymes through the duplex is involved. We propose a threestep mechanism in which DEAD-box proteins unwind duplexes as local strand separators. This unwinding mode is well-suited for local structural changes in complex RNA or RNP assemblies.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available