Characterization of endonuclease activities in Moloney murine leukemia virus and its replication-defective mutants
- Creators
- Panet, Amos
- Baltimore, David
Abstract
To study Moloney murine leukemia virus (M-MulV) proteins associated with the integration of proviral DNA into the host chromosome, we isolated endonuclease activities from purified virion preparations of the wild type and two of its replication mutants. A major endonuclease activity was identified in virions of M-MuLV; the enzyme catalyzed nicks in double-stranded DNA in the presence of either Mn2+ or Mg2+ and was stimulated by ATP. The endonuclease nicked DNA adjacent to all four nucleotides with some preference for G and C. The same enzyme, and in comparable amounts, was isolated from two virus replication mutants: dl2905, deficient in the processing of Pr65gag and Pr200gag-pol, and dl50401, deficient for the virus integration function. In the process of these experiments, the residual reverse transcriptase in mutant dl2905 was shown to be the mature size, implying that the uncleaved precursor lacks enzymatic activity. It appears that the major endonuclease activity found in virions of M-MuLV is not encoded by either the gag or pol genes.
Additional Information
Copyright © 1987 by the American Society for Microbiology. Received 6 August 1986/Accepted 2 February 1987 A.P. was supported by the Eleanor Roosevelt International Fellowship of the International Union Against Cancer. This investigation was supported by Public Health Service grant CA 38497-02 from the National Institutes of Health. We thank S. Goff for providing cell lines and Paul Matsudaira for helpful discussions.Files
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Additional details
- Eprint ID
- 2521
- Resolver ID
- CaltechAUTHORS:PANjvir87
- Created
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2006-04-06Created from EPrint's datestamp field
- Updated
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2019-10-02Created from EPrint's last_modified field