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Bacteriophage-induced inhibitor of a host enzyme

Technical Report ·
DOI:https://doi.org/10.2172/7293002· OSTI ID:7293002
Bacillus subtilis bacteriophage PBS2 is unique among viruses in that its DNA contains uracil instead of thymine. It is of interest to determine how and why PBS2 contains this unusual base in its DNA. New proteins induced after infection of B. subtilis by PBS2 phage include: dTMP 5'-phosphatase, which also has dUMP 5'-phosphatase activity; dCTP deaminase; dUMP kinase; DNA polymerase; RNA polymerase; an inhibitor of the host's deoxyribonuclease specific for uracil-containing DNA; and an inhibitor of the host's N/glycosidase specific for uracil-containing DNA. The paper describes the discovery of another PBS2 protein; a phage-induced inhibitor of the B. subtilis deoxyuridinetriphosphatase (dUTPase). The cellular dUTPase is thought to help exclude uracil from B. subtilis DNA, by hydrolyzing dUTP to dUMP plus PP/sub i/. It is believed that an important function for PBS2 phage is to inhibit the host's dUTPase, thereby allowing dUTP to accumulate for the synthesis of PBS2 uracil-containing DNA.
Research Organization:
Michigan Univ., Ann Arbor (USA). Dept. of Biological Chemistry
Sponsoring Organization:
US Energy Research and Development Administration (ERDA)
OSTI ID:
7293002
Report Number(s):
COO-2101-26
Country of Publication:
United States
Language:
English