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© Research
Publication : Extremophiles : life under extreme conditions

Characterization of Sulfolobus islandicus rod-shaped virus 2 gp19, a single-strand specific endonuclease

Team: Archived: Viruses of Hyperthermophilic Archaea
Team: Archived: Molecular Biology of Gene in Extremophiles
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Extremophiles : life under extreme conditions - 11 Jun 2011

Gardner AF, Prangishvili D, Jack WE

Link to Pubmed [PMID] – 21667093

Extremophiles 2011 Sep;15(5):619-24

The hyperthermophilic Sulfolobus islandicus rod-shaped virus 2 (SIRV2) encodes a 25-kDa protein (SIRV2gp19) annotated as a hypothetical protein with sequence homology to the RecB nuclease superfamily. Even though SIRV2gp19 homologs are conserved throughout the rudivirus family and presumably play a role in the viral life cycle, SIRV2gp19 has not been functionally characterized. To define the minimal requirements for activity, SIRV2gp19 was purified and tested under varying conditions. SIRV2gp19 is a single-strand specific endonuclease that requires Mg(2+) for activity and is inactive on double-stranded DNA. A conserved aspartic acid in RecB nuclease superfamily Motif II (D89) is also essential for SIRV2gp19 activity and mutation to alanine (D89A) abolishes activity. Therefore, the SIRV2gp19 cleavage mechanism is similar to previously described RecB nucleases. Finally, SIRV2gp19 single-stranded DNA endonuclease activity could play a role in host chromosome degradation during SIRV2 lytic infection.