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

T. Restle; B. Müller; R. S. Goody

doi:10.1016/0014-5793(92)80172-D

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

T. Restle^*, B. Müller, R. S. Goody

^*Corresponding author for this work

Institute of Molecular Medicine

Max Planck-Institute for Medical Research

63 Citations (Scopus)

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.

Original language	English
Journal	FEBS Letters
Volume	300
Issue number	1
Pages (from-to)	97-100
Number of pages	4
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(92)80172-D
Publication status	Published - 23.03.1992

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1016/0014-5793(92)80172-D

Cite this

@article{e6700e5437504c589a584f6eac628098,

title = "RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms",

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.",

author = "T. Restle and B. M{\"u}ller and Goody, {R. S.}",

year = "1992",

month = mar,

day = "23",

doi = "10.1016/0014-5793(92)80172-D",

language = "English",

volume = "300",

pages = "97--100",

journal = "FEBS Letters",

issn = "0014-5793",

number = "1",

}

TY - JOUR

T1 - RNase H activity of HIV reverse transcriptases is confined exclusively to the dimeric forms

AU - Restle, T.

AU - Müller, B.

AU - Goody, R. S.

PY - 1992/3/23

Y1 - 1992/3/23

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0026503970&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(92)80172-D

DO - 10.1016/0014-5793(92)80172-D

M3 - Journal articles

C2 - 1372272

AN - SCOPUS:0026503970

SN - 0014-5793

VL - 300

SP - 97

EP - 100

JO - FEBS Letters

JF - FEBS Letters

IS - 1

ER -

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

Abstract

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this