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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1996-3-11
|
| pubmed:abstractText |
In this investigation, we examine the interaction between the human immunodeficiency virus type I integrase and oligonucleotides that reflect the sequences of the extreme termini of the viral long terminal repeats (LTRs). The results of gel filtration and a detailed binding density analysis indicate that the integrase binds to the LTR as a high-order oligomer at a density equivalent to 10 +/- 0.8 integrase monomers per 21-base pair LTR. The corresponding binding isotherm displays a Hill coefficient of 2, suggesting that the binding mechanism involves the cooperative interaction between two oligomers. This interaction is quite stable, exhibiting a prolonged half-life (t1/2 approximately 13 h) in the presence of Mn2+ cations. Complexes were less stable when formed with Mg2+ (t1/2 approximately 1 h). The role of Mn2+ appears to be in the induction of the protein-protein interactions that stabilize the bound complexes. In terms of the 3'-end processing of the LTR, similar catalytic rates (kcat approximately 0.06 min-1) were obtained for the stable complex in the presence of either cation. Hence, the apparent preference observed for Mn2+ in standard in vitro integration assays can be attributed entirely to the augmentation in the DNA binding affinity of the integrase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Integrases,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Manganese,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
19
|
| pubmed:volume |
271
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1498-506
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8576144-Base Sequence,
pubmed-meshheading:8576144-Binding Sites,
pubmed-meshheading:8576144-Cations, Divalent,
pubmed-meshheading:8576144-DNA, Viral,
pubmed-meshheading:8576144-DNA Nucleotidyltransferases,
pubmed-meshheading:8576144-HIV Long Terminal Repeat,
pubmed-meshheading:8576144-HIV-1,
pubmed-meshheading:8576144-Humans,
pubmed-meshheading:8576144-Integrases,
pubmed-meshheading:8576144-Kinetics,
pubmed-meshheading:8576144-Magnesium,
pubmed-meshheading:8576144-Manganese,
pubmed-meshheading:8576144-Mathematics,
pubmed-meshheading:8576144-Models, Theoretical,
pubmed-meshheading:8576144-Molecular Sequence Data,
pubmed-meshheading:8576144-Oligodeoxyribonucleotides,
pubmed-meshheading:8576144-Recombinant Proteins,
pubmed-meshheading:8576144-Substrate Specificity,
pubmed-meshheading:8576144-Time Factors,
pubmed-meshheading:8576144-Virus Integration
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
The metal ion-induced cooperative binding of HIV-1 integrase to DNA exhibits a marked preference for Mn(II) rather than Mg(II).
|
| pubmed:affiliation |
Unité de Physicochimie des Macromolécules Biologiques CNRS URA 1149, Institut Pasteur, Paris, France.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|