Temperature-sensitive DNA polymerase induced by a bacteriophage T5 mutant: relationship between polymerase and exonuclease activities.

Fujimura RK, Roop BC
Biochemistry (1976), Volume 15, Page 4403
PubMed entry


DNA polymerase induced by bacteriophage T5ts53, a mutant with ...
DNA polymerase induced by bacteriophage T5ts53, a mutant with temperature-sensitive polymerase, was purified to about 95% purity as judged by dodecyl sulfate gel electrophoresis. The 3' leads to 5' exonuclease associated with the polymerase had higher activity than that associated with the parent wild-type enzyme. It was more stable to heat than the polymerase, and it degraded primer-template even in the presence of 4 dNTP's at higher temperature. However, the evidence presented shows that the inhibition of DNA synthesis by higher temperature was primarily due to defects in polymerase function rather than to overactive exonuclease. The presence of primer-template DNA stabilized the polymerase to heat. Purified ts53 polymerase was also shown to discriminate against incorportion of BrdUMP, especially at higher temperature. This is an agreement with observations made in vivo with ts53-infected bacteria.




new topics/pols set partial results complete validated


No results available for this paper.

Entry validated by:

Using Polbase tables:


Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).


It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.