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

^*Korrespondierende/r Autor/-in für diese Arbeit

Max Planck-Institut für Medizinische Forschung

70 Zitate (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.

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	300
Ausgabenummer	1
Seiten (von - bis)	97-100
Seitenumfang	4
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(92)80172-D
Publikationsstatus	Veröffentlicht - 23.03.1992

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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",

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AU - Müller, B.

AU - Goody, R. S.

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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 - https://www.scopus.com/pages/publications/0026503970

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

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JO - FEBS Letters

JF - FEBS Letters

IS - 1

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

Abstract

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