Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1995-11-30
pubmed:abstractText
The binding of HIV reverse transcriptase (RT) to heteroduplexes was examined using a substrate consisting of a 42 nt chimeric nucleic acid composed. (5'-->3') of 23 nt of RNA and 19 of DNA. This chimera was hybridized to an internal region of a relatively long complementary DNA or RNA. When the chimera was bound to DNA and conditions limiting cleavage to a single binding event between the enzyme and substrate were employed initial RNase H-directed cleavages occurred 19-21 nt from the chimera 5'-terminus. A 42 nt strand identical in sequence to the chimera and composed of only RNA was cleaved at the same locations. Reducing the length of the DNA portion of the chimera from 19 to 7 nt did not alter the cleavage positions, suggesting that cleavage was not coordinated by the DNA 3'-terminus. Under the same conditions cleavage was not detected when the chimera was bound to RNA. In contrast, addition of dNTPs to the DNA 3'-terminus of the chimera occurred only when the chimera was bound to RNA. The results support preferable binding of RT to RNA-DNA versus DNA-DNA hybrid regions and a model in which the orientation of binding to heteroduplexes is 5'-->3' (relative to the RNA strand), polymerase to RNase H active site, with sites associated with the DNA and RNA strand respectively.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1279694, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1279806, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1281479, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1371014, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1376369, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1377403, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1560526, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1693920, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1694894, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1701399, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1702425, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1703002, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-1722202, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-2418504, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-2442162, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-2468665, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-6092661, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-6176578, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-6197536, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-6199510, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-6202882, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-6206236, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-7682554, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-7687463, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-7692401, http://linkedlifedata.com/resource/pubmed/commentcorrection/7479034-88956
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0305-1048
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3901-8
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The orientation of binding of human immunodeficiency virus reverse transcriptase on nucleic acid hybrids.
pubmed:affiliation
Department of Microbiology, University of Maryland, College Park 20742, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.