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An Expanded Model of Replicating Human Immunodeficiency Virus Reverse Transcriptase

Title data

Wöhrl, Birgitta M. ; Tantillo, Chris ; Arnold, Edward ; Le Grice, Stuart F.J.:
An Expanded Model of Replicating Human Immunodeficiency Virus Reverse Transcriptase.
In: Biochemistry. Vol. 34 (1995) Issue 16 . - pp. 5343-5350.
ISSN 1520-4995
DOI: https://doi.org/10.1021/bi00016a005

Abstract in another language

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 SI 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 synthes is 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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers > Lehrstuhl Biopolymere - Apl. Prof. Dr. Birgitta Wöhrl
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 20 May 2019 07:56
Last Modified: 20 May 2019 07:56
URI: https://eref.uni-bayreuth.de/id/eprint/48998