Work

Bacterial-type DNA Holliday junction resolvases in eukaryotic viruses

Year: 2000

Type: article

Abstract: Homologous DNA recombination promotes genetic diversity and the maintenance of genome integrity, yet no enzymes with specificity for the Holliday junction (HJ)-a key DNA recombination intermediate-have been purified and characterized from metazoa or their viruses. Here we identify critical structural elements of RuvC, a bacterial HJ resolvase, in uncharacterized open reading frames from poxviruses and an iridovirus. The putative vaccinia virus resolvase was expressed as a recombinant protein, affinity purified, and shown to specifically bind and cleave a synthetic HJ to yield nicked duplex molecules. Mutation of either of two conserved acidic amino acids abrogated the catalytic activity of the A22R protein without affecting HJ binding. The presence of bacterial-type enzymes in metazoan viruses raises evolutionary questions.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.150238697

Authors: Alonzo D. Garcia, L. Aravind, Eugene V. Koonin, Bernard Moss

Institutions: National Institutes of Health, National Center for Biotechnology Information, National Institute of Allergy and Infectious Diseases

Language: English

Topic: Poxvirus research and outbreaks

Subfield: Virology

Field: Immunology and Microbiology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W1975384668

FWCI: 3.3

Cites: 43

Cited by: 108

Related to: 10