Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1995-6-1
pubmed:abstractText
Replication complexes containing wild-type and RNase H-deficient p66/p51 human immunodeficiency virus type 1 reverse transcriptase (HIV-1 RT) were analyzed by DNase I and S1 footprinting. While crystallography and chemical footprinting data demonstrate that 15-18 bases of primer and template occupy the DNA polymerase and RNase H active centers, enzymatic footprinting suggests that a larger portion of substrate is encompassed by the replicating enzyme. Independent of the position of DNA synthesis arrest, template nucleotides +7 to -23 and primer nucleotides -1 to -25 are nuclease resistant. On both DNA strands, position -20 remains accessible to DNase I cleavage, suggestive of an alteration in nucleic acid structure between exiting the RNase H catalytic center and leaving the C-terminal p66 domain. A model of HIV-1 RT containing an extended single-stranded template and duplex region was constructed on the basis of the structure of an RT/DNA complex. Mapping of footprint data onto this model shows consistency between biochemical and structural data, implicating a contribution from domains proximal to the catalytic centers.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5343-56
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:7537089-Base Sequence, pubmed-meshheading:7537089-Binding Sites, pubmed-meshheading:7537089-DNA, Viral, pubmed-meshheading:7537089-DNA Primers, pubmed-meshheading:7537089-DNA Replication, pubmed-meshheading:7537089-DNA-Directed DNA Polymerase, pubmed-meshheading:7537089-Deoxyribonuclease I, pubmed-meshheading:7537089-HIV Reverse Transcriptase, pubmed-meshheading:7537089-HIV-1, pubmed-meshheading:7537089-Models, Molecular, pubmed-meshheading:7537089-Molecular Sequence Data, pubmed-meshheading:7537089-Nucleic Acid Conformation, pubmed-meshheading:7537089-Protein Conformation, pubmed-meshheading:7537089-Protein Structure, Secondary, pubmed-meshheading:7537089-RNA-Directed DNA Polymerase, pubmed-meshheading:7537089-Recombinant Proteins, pubmed-meshheading:7537089-Ribonuclease H, pubmed-meshheading:7537089-Substrate Specificity, pubmed-meshheading:7537089-Templates, Genetic
pubmed:year
1995
pubmed:articleTitle
An expanded model of replicating human immunodeficiency virus reverse transcriptase.
pubmed:affiliation
Division of Infectious Diseases, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't