Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1996-10-17
pubmed:abstractText
The reverse transcriptase (RT) of the human immunodeficiency virus type 1 (HIV-1) is composed of two subunits of 66 and 51 kDa in a 1 to 1 ratio. Because dimerization is a prerequisite for enzymatic activity, interference with the dimerization process could constitute an alternative antiviral strategy for RT inhibition. Here we describe an in vitro assay for the study of the dimerization state of HIV-1 reverse transcriptase based on chemical crosslinking of the subunits with dimethylsuberimidate. Crosslinking results in the formation of covalent bonds between the subunits, so that the crosslinked species can be resolved by denaturing gel electrophoresis. Crosslinked RT species with molecular weight greater than that of the dimeric form accumulate during a 1-15-min time course. Initial evidence suggests that those high molecular weight species represent trimers and tetramers and may be the result of intramolecular crosslinking of the subunits of a higher-order RT oligomer. A peptide that corresponds to part of the tryptophan repeat motif in the connection domain of HIV-1 RT inhibits crosslink formation as well as enzymatic activity. The crosslinking assay thus allows the investigation of the effect of inhibitors on the dimerization of HIV-1 RT.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1370707, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1371690, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1377403, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1379251, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1689015, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1693146, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1694894, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1698361, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1701568, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1706608, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1721535, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-1722701, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-2423366, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-2429313, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-2430111, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-2452083, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-409338, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-4913206, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7513698, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7523383, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7529365, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7530020, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7530541, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7682251, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7687065, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7688571, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7694651, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-7816094, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-8455722, http://linkedlifedata.com/resource/pubmed/commentcorrection/8745406-8486715
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0961-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
278-86
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Chemical crosslinking of the subunits of HIV-1 reverse transcriptase.
pubmed:affiliation
Rega Institute for Medical Research, Leuven, Belgium. zegerdebyser@uz.kuleuven.ac.be
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't