Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Henn A,Cao W,Licciardello N,Heitkamp SE,Hackney DD,De La Cruz EMdoi
10.1073/pnas.0913081107subject
Has Abstractpub_date
2010-03-02 00:00:00pages
4046-50issue
9eissn
0027-8424issn
1091-6490pii
0913081107journal_volume
107pub_type
杂志文章abstract::The bacteriophage T4-encoded RegB endoribonuclease is produced during the early stage of phage development and targets mostly (but not exclusively) the Shine-Dalgarno sequences of early genes. In this work, we show that the degradation of RegB-cleaved mRNAs depends on a functional T4 polynucleotide kinase/phosphatase ...
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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