Temperature-sensitive dna polymerase from rous sarcoma virus mutants
✍ Scribed by David Baltimore; Inder M. Verma; Stanley Drost; William S. Mason
- Publisher
- John Wiley and Sons
- Year
- 1974
- Tongue
- English
- Weight
- 251 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0008-543X
No coin nor oath required. For personal study only.
✦ Synopsis
T h e DNA polymerase ("reverse transcriptase") has been isolated from virions of two temperature-sensitive Rous sarcoma virus mutants (ts335 a n d ts337). These mutants are defective a t a n early stage of both growth a n d transformation. The purified polymerase is three-fold more rapidly inactivated by heat than is wild type polymerase. T h e ribonuclease H activity of the mutant enzyme also shows a n increased heat-lability when compared to the wild type activity. Studies on recombinants of the mutants with an avian leukosis virus indicate that the defects in growth and trankformation are caused by the heat-lability of the DNA polymerase. These studies strongly support the idea that the virion DNA polymerase of RNA tumor virus is needed to synthesize a DNA copy of the viral genome soon after the infection of a cell by an RNA tumor virus.
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