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PMID: 1372272 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms.

FEBS letters ·Vol. 300 ·No. 1 ·1992-03-23 ·Pages 97-100

Restle T, Müller B, Goody RS

Abstract

A method for the rapid preparation of a defined substrate to monitor RNase H activity has been developed. Using this substrate, we have investigated the RNase H activities of the different forms of recombinant HIV-1 and HIV-2 reverse transcriptase (RT) in detail. As we report here, RNase H activity is associated only with the dimeric forms (p51/p66 or p66/p66) of the enzymes.

MeSH Terms

Amino Acid Sequence HIV/enzymology Molecular Sequence Data RNA-Directed DNA Polymerase/chemistry,metabolism Ribonuclease H/metabolism

Chemicals

RNA-Directed DNA Polymerase Ribonuclease H

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Restle T

Abteilung Biophysik, Max-Planck-Institut für medizinische Forschung, Heidelberg, Germany.

Müller B

Goody R S

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(92)80172-d

Published

1992-03-23

Pages

97-100

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(92)80172-d View journal details

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RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms.

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