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Stable complexes formed by HIV-1 reverse transcriptase at distinct positions on the primer-template controlled by binding deoxynucleoside triphosphates or foscarnet
- Source :
- Journal of molecular biology. 369(1)
- Publication Year :
- 2007
-
Abstract
- Binding of the next complementary dNTP by the binary complex containing HIV-1 reverse transcriptase (RT) and primer-template induces conformational changes that have been implicated in catalytic function of RT. We have used DNase I footprinting, gel electrophoretic mobility shift, and exonuclease protection assays to characterize the interactions between HIV-1 RT and chain-terminated primer-template in the absence and presence of various ligands. Distinguishable stable complexes were formed in the presence of foscarnet (an analogue of pyrophosphate), the dNTP complementary to the first (+1) templating nucleotide or the dNTP complementary to the second (+2) templating nucleotide. The position of HIV-1 RT on the primer-template in each of these complexes is different. RT is located upstream in the foscarnet complex, relative to the +1 complex, and downstream in the +2 complex. These results suggest that HIV-1 RT can translocate along the primer-template in the absence of phosphodiester bond formation. The ability to form a specific foscarnet complex might explain the inhibitory properties of this compound. The ability to recognize the second templating nucleotide has implications for nucleotide misincorporation.
- Subjects :
- Exonuclease
Foscarnet
DNA, Complementary
Stereochemistry
DNA Footprinting
Pyrophosphate
Article
chemistry.chemical_compound
Structural Biology
medicine
Deoxyribonuclease I
Nucleotide
Molecular Biology
DNA Primers
chemistry.chemical_classification
biology
Nucleotides
DNase-I Footprinting
virus diseases
Templates, Genetic
Molecular biology
Reverse transcriptase
HIV Reverse Transcriptase
Exodeoxyribonucleases
chemistry
Phosphodiester bond
biology.protein
Primer (molecular biology)
medicine.drug
Protein Binding
Subjects
Details
- ISSN :
- 00222836
- Volume :
- 369
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Journal of molecular biology
- Accession number :
- edsair.doi.dedup.....1f921b1ef58cd29f932f95ad0aa6fa50