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A DNA nicking-closing enzyme encapsidated in vaccinia virus: partial purification and properties.

Authors
  • Bauer, W R
  • Ressner, E C
  • Kates, J
  • Patzke, J V
Type
Published Article
Journal
Proceedings of the National Academy of Sciences of the United States of America
Publication Date
May 01, 1977
Volume
74
Issue
5
Pages
1841–1845
Identifiers
PMID: 17115
Source
Medline
License
Unknown

Abstract

Vaccinia virus cores contain an activity which is able to relax both left-and right-handed superhelical DNA. This virus-specific nicking closing enzyme has been highly purified and differs from the corresponding host enzyme in salt optimum, in sedimentation coefficient, and in polypeptide composition as determined on sodium dodecyl sulfate/polyacrylamide gels. The enzyme is probably newly synthesized after the cessation of host protein synthesis which follows virus infection. The most highly purified preparation contains two polypeptides, one of molecular weight 24,000 and the other 35,000. The former polypeptide is a major constituent of the virus (7% of total protein by weight), whereas the latter is present in a much smaller amount (0.2%). Chromatography with denatured DNA-cellulose reveals that the activity is predominately associated with those fractions enriched in the polypeptide of greater molecular weight.

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