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The Dead Box Helicase YxiN Maintains a Closed Conformation during ATP Hydrolysis

Aregger, R. and Klostermeier, D.. (2009) The Dead Box Helicase YxiN Maintains a Closed Conformation during ATP Hydrolysis. Biochemistry, Vol. 48, H. 45. pp. 10679-10681.

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Official URL: http://edoc.unibas.ch/dok/A5259697

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Abstract

DEAD box helicases unwind RNA duplexes at the expense of ATP hydrolysis. Recently, unwinding has been demonstrated in the absence of ATP hydrolysis. Herein, we show that ADP.BeF(x) supports RNA unwinding by YxiN, a DEAD box helicase that specifically recognizes a hairpin in 23S rRNA. ADP.AlF(x) and ADP.MgF(x) do not promote RNA unwinding, but all ATP analogues induce a closed conformation of the helicase core as required for RNA unwinding. Our results show that the interdomain cleft in the helicase core closes upon ATP binding at the beginning of the cycle. Reopening occurs after ATP hydrolysis, most likely coupled to phosphate release.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Biophysical Chemistry (Klostermeier)
UniBasel Contributors:Klostermeier, Dagmar
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:American Chemical Society
ISSN:0006-2960
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:21
Deposited On:22 Mar 2012 13:23

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