Linked Life Data

10911996

Source:http://linkedlifedata.com/resource/pubmed/id/10911996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2000-8-15
pubmed:databankReference
pubmed:abstractText
Transposition requires a coordinated series of DNA breakage and joining reactions. The Tn7 transposase contains two proteins: TnsA, which carries out DNA breakage at the 5' ends of the transposon, and TnsB, which carries out breakage and joining at the 3' ends of the transposon. TnsB is a member of the retroviral integrase superfamily whose hallmark is a conserved DDE motif. We report here the structure of TnsA at 2.4 A resolution. Surprisingly, the TnsA fold is that of a type II restriction endonuclease. Thus, Tn7 transposition involves a collaboration between polypeptides, one containing a DDE motif and one that does not. This result indicates that the range of biological processes that utilize restriction enzyme-like folds also includes DNA transposition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1025-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10911996-Bacterial Proteins, pubmed-meshheading:10911996-Binding Sites, pubmed-meshheading:10911996-Catalytic Domain, pubmed-meshheading:10911996-Crystallography, X-Ray, pubmed-meshheading:10911996-DNA, pubmed-meshheading:10911996-DNA Transposable Elements, pubmed-meshheading:10911996-DNA-Binding Proteins, pubmed-meshheading:10911996-Deoxyribonucleases, Type II Site-Specific, pubmed-meshheading:10911996-Escherichia coli Proteins, pubmed-meshheading:10911996-Magnesium, pubmed-meshheading:10911996-Models, Molecular, pubmed-meshheading:10911996-Mutation, pubmed-meshheading:10911996-Protein Folding, pubmed-meshheading:10911996-Protein Structure, Secondary, pubmed-meshheading:10911996-Recombination, Genetic, pubmed-meshheading:10911996-Structure-Activity Relationship, pubmed-meshheading:10911996-Transposases
pubmed:year
2000
pubmed:articleTitle
Unexpected structural diversity in DNA recombination: the restriction endonuclease connection.
pubmed:affiliation
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. ahickman@helix.nih.gov
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't