Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
22
pubmed:dateCreated
1995-11-30
pubmed:abstractText
Integration of human immunodeficiency virus type 1 cDNA into a target DNA can be strongly influenced by the conformation of the target. For example, integration in vitro is sometimes favored in target DNAs containing sequence-directed bends or DNA distortions caused by bound proteins. We have analyzed the effect of DNA bending by studying integration into two well-characterized protein-DNA complexes: Escherichia coli integration host factor (IHF) protein bound to a phage IHF site, and the DNA binding domain of human lymphoid enhancer factor (LEF) bound to a LEF site. Both of these proteins have previously been reported to bend DNA by approximately 140 degrees. Binding of IHF greatly increases the efficiency of in vitro integration at hotspots within the IHF site. We analyzed a series of mutants in which the IHF site was modified at the most prominent hotspot. We found that each variant still displayed enhanced integration upon IHF binding. Evidently the local sequence is not critical for formation of an IHF hotspot. LEF binding did not create preferred sites for integration. The different effects of IHF and LEF binding can be rationalized in terms of the different proposed conformations of the two protein-DNA complexes.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-1317268, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-1319063, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-1548767, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-1555239, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-1847518, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-1870194, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2083253, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2164223, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2166364, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2167180, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2170022, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2214029, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2235486, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2541927, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2544029, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2831189, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-2972993, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-3340190, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-6096022, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-6540370, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-7651541, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-7774012, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-7774816, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-7925312, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-7929189, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-7937746, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-7991603, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-8016088, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-8041787, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-8126009, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-8202527, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-8253387, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479779-8265659
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10334-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:7479779-Bacterial Proteins, pubmed-meshheading:7479779-Base Sequence, pubmed-meshheading:7479779-DNA, Complementary, pubmed-meshheading:7479779-DNA, Viral, pubmed-meshheading:7479779-DNA Nucleotidyltransferases, pubmed-meshheading:7479779-DNA Primers, pubmed-meshheading:7479779-DNA-Binding Proteins, pubmed-meshheading:7479779-HIV-1, pubmed-meshheading:7479779-Humans, pubmed-meshheading:7479779-Integrases, pubmed-meshheading:7479779-Integration Host Factors, pubmed-meshheading:7479779-Models, Structural, pubmed-meshheading:7479779-Molecular Sequence Data, pubmed-meshheading:7479779-Nucleic Acid Conformation, pubmed-meshheading:7479779-Polymerase Chain Reaction, pubmed-meshheading:7479779-Protein Conformation, pubmed-meshheading:7479779-Recombinant Proteins, pubmed-meshheading:7479779-Virus Integration
pubmed:year
1995
pubmed:articleTitle
In vitro integration of human immunodeficiency virus type 1 cDNA into targets containing protein-induced bends.
pubmed:affiliation
Salk Institute for Biological Studies, San Diego, CA 92186-8500, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.