Linked Life Data

7640275

Source:http://linkedlifedata.com/resource/pubmed/id/7640275

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1995-9-19
pubmed:abstractText
Human immunodeficiency virus type 1 integrase (HIV-1 IN) catalyzes the integration of HIV-1 DNA into the host chromosome. In vitro reactions with endogenous viral DNA require Mg2+ as the metal cofactor, whereas in vitro studies performed with short oligonucleotide substrates utilize Mn2+. In this study, we report that the donor processing activity of HIV-1 IN alters depending on the structure and length of the oligonucleotide substrates. Increases in the length of the substrate cause alterations in the efficiency of Mg(2+)-dependent donor processing activity, thereby reconciling this discrepancy between the in vivo and in vitro HIV-1 IN mediated reactions. We have also found that the 3'-processing activity of HIV-IN is responsible for cleaving the junction between the viral and target sequences of the recombination intermediate. Its mechanism differs from the previously described disintegration reaction in that the donor strands are regenerated without a joining reaction of the target strands. Kinetic studies of 3'-processing activity suggest that the kcat (0.24/h) is very low. This implies that HIV-1 IN remains as a complex with the processed DNA prior to the strand transfer reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10205-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Characterization of Mg(2+)-dependent 3'-processing activity for human immunodeficiency virus type 1 integrase in vitro: real-time kinetic studies using fluorescence resonance energy transfer.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington, D.C. 20007, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't