Efficient Magnesium-dependent Human Immunodeficiency Virus Type 1 Integrase Activity

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 1995 Sep 1

PMID 7637039

Citations 28

Authors

A Engelman

R Craigie

Affiliations

Soon will be listed here.

Abstract

The integrase protein from human immunodeficiency virus type 1 (HIV-1) has generally been reported to require Mn2+ for efficient in vitro activity. We have reexamined the divalent metal ion requirements of HIV-1 integrase and find that the protein is capable of promoting efficient 3' processing and DNA strand transfer with either Mn2+ or Mg2+. The metal ion preference depended upon the reaction conditions. HIV-1 integrase displayed significantly less nonspecific nuclease activity in reaction mixtures containing Mg2+ than it did under the previously described reaction conditions with mixtures containing Mn2+.

Citing Articles

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Retroviral DNA Integration.

Lesbats P, Engelman A, Cherepanov P Chem Rev. 2016; 116(20):12730-12757.

PMID: 27198982 PMC: 5084067. DOI: 10.1021/acs.chemrev.6b00125.

Integrase-mediated spacer acquisition during CRISPR-Cas adaptive immunity.

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Biochemical characterization of novel retroviral integrase proteins.

Ballandras-Colas A, Naraharisetty H, Li X, Serrao E, Engelman A PLoS One. 2013; 8(10):e76638.

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3'-processing and strand transfer catalysed by retroviral integrase in crystallo.

Hare S, Maertens G, Cherepanov P EMBO J. 2012; 31(13):3020-8.

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