Linked Life Data

15837195

Source:http://linkedlifedata.com/resource/pubmed/id/15837195

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-4-19
pubmed:abstractText
The open/closed transition in polymerases is a crucial event in DNA replication and transcription. We hypothesize that the residues that transmit the signal for the open/closed transition are also strongly conserved. To identify the dynamically relevant residues, we use an elastic network model of polymerases and probe the residue-specific response to a local perturbation. In a variety of DNA/RNA polymerases, a network of residues spanning the fingers and palm domains is involved in the open/closed transition. The similarity in the network of residues responsible for large-scale domain movements supports the notion of a common induced-fit mechanism in the polymerase families for the formation of a closed ternary complex. Multiple sequence alignment shows that many of these residues are also strongly conserved. Residues with the largest sensitivity to local perturbations include those that are not so obviously involved in the polymerase catalysis. Our results suggest that mutations of the mechanical "hot spots" can compromise the efficiency of the enzyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
565-77
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Network of dynamically important residues in the open/closed transition in polymerases is strongly conserved.
pubmed:affiliation
Laboratory of Computational Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. zhengwj@helix.nih.gov
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.