期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 9, 页码 4046-4050出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0913081107
关键词
ATPase; kinetics; Molecular Motor; RNA helicase
资金
- National Science Foundation (NSF) [MCB-0546353, MCB-0615549, DGE-0644492]
- National Institutes of Health [GM071688]
- AHA [X0625997T]
- Raymond and Beverly Sackler Institute
- [0940075N]
DEAD-box RNA helicase proteins use the energy of ATP hydrolysis to drive the unwinding of duplex RNA. However, the mechanism that couples ATP utilization to duplex RNA unwinding is unknown. We measured ATP utilization and duplex RNA unwinding by DbpA, a non-processive bacterial DEAD-box RNA helicase specifically activated by the peptidyl transferase center (PTC) of 23S rRNA. Consumption of a single ATP molecule is sufficient to unwind and displace an 8 base pair rRNA strand annealed to a 32 base pair PTC-RNA mother strand fragment. Strand displacement occurs after ATP binding and hydrolysis but before P-i product release. P-i release weakens binding to rRNA, thereby facilitating the release of the unwound rRNA mother strand and the recycling of DbpA for additional rounds of unwinding. This work explains how ATPase activity of DEAD-box helicases is linked to RNA unwinding.
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