|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2010-3-1
|
|
pubmed:abstractText |
RNA helicases function in numerous aspects of RNA biology. These enzymes are RNA-stimulated ATPases that translocate on RNA and unwind or remodel structured RNA in an ATP-dependent fashion. How ATP and the ATPase cycle fuel the work performed by helicases is not completely clear. The hepatitis C virus RNA helicase, NS3, is an important model system for this class of enzymes. NS3 binding to a single-/double-strand RNA or DNA junction leads to ATP-independent melting of the duplex and formation of a complex capable of ATP-dependent unwinding by using a spring-loaded mechanism. We have established an RNA substrate for NS3 that can be unwound in a single sub-step. Our studies are consistent with a model in which a single ATP binding and/or hydrolysis event sets the unwinding spring and phosphate dissociation contributes to release of the spring, thereby driving the power stroke used for unwinding.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-10390360,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-10681506,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-11152498,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-11861865,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-11867545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-12162749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-12504562,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-15269774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-15634684,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-15806107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-15915565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-16126720,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-16246727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-16306038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-16397502,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-17084859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-17504766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-17656723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-17679086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-17709749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-17964264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-18155046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-18179252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-18237742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-18283103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-18497749,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-18573084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-19010782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-19088196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-19088201,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-4202581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-7854446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-8031761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-8798703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19969541-9516436
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
1362-4962
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:volume |
38
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1312-24
|
|
pubmed:dateRevised |
2010-9-27
|
|
pubmed:meshHeading |
|
|
pubmed:year |
2010
|
|
pubmed:articleTitle |
Phosphate release contributes to the rate-limiting step for unwinding by an RNA helicase.
|
|
pubmed:affiliation |
Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|
