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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2011-06-11

AUTHORS

Andrew F. Gardner, David Prangishvili, William E. Jack

ABSTRACT

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. More... »

PAGES

619-624

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00792-011-0385-0

DOI

http://dx.doi.org/10.1007/s00792-011-0385-0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028833206

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/21667093


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