Linked Life Data

21350762

Source:http://linkedlifedata.com/resource/pubmed/id/21350762

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
21
pubmed:dateCreated
2011-5-19
pubmed:abstractText
Reverse gyrase introduces positive supercoils into DNA in an ATP-dependent process. It has a modular structure comprising a helicase-like and a topoisomerase domain. The helicase-like domain consists of two RecA-like subdomains and thus structurally resembles members of the helicase superfamily 2. It is a nucleotide-dependent switch that alters between an ATP state with a slight preference for dsDNA, and an ADP state with a high preference for ssDNA. Inter-domain communication between the helicase-like and the topoisomerase domain is central for their functional cooperation in reverse gyrase. The latch, an insertion into the helicase-like domain, has been suggested as an important element in coordinating their activities. Here, we have dissected the nucleotide cycle of the reverse gyrase helicase-like domain in the absence and presence of different DNA substrates. With this comprehensive thermodynamic characterization of the nucleotide cycle of the helicase-like domain, in combination with single molecule FRET data on the conformation of the helicase-like domain at all stages of the catalytic cycle, a picture emerges as to how the helicase-like domain may guide ATP-dependent positive supercoiling by reverse gyrase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1463-9084
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10009-19
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Nucleotide-driven conformational changes in the reverse gyrase helicase-like domain couple the nucleotide cycle to DNA processing.
pubmed:affiliation
University of Basel, Biozentrum, Dept. of Biophysical Chemistry, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't