Title : Bacillus subtilis deoxyuridinetriphosphatase and its bacteriophage PBS2-induced inhibitor.

Pub. Date : 1975 Nov 25

PMID : 810487






4 Functional Relationships(s)
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1 We propose that infection at high pH prevents the PBS2-induced dUTPase inhibitor from blocking the B. subtilis dUTPase activity, thereby allowing the degradation of dUTP and the synthesis of dTTP (both of which are DNA polymerase substrates), so that thymine replaces some of the uracil normally found in PBS2 DNA. pbs2 Deoxyuridine triphosphatase Drosophila melanogaster
2 We propose that infection at high pH prevents the PBS2-induced dUTPase inhibitor from blocking the B. subtilis dUTPase activity, thereby allowing the degradation of dUTP and the synthesis of dTTP (both of which are DNA polymerase substrates), so that thymine replaces some of the uracil normally found in PBS2 DNA. pbs2 Deoxyuridine triphosphatase Drosophila melanogaster
3 We propose that infection at high pH prevents the PBS2-induced dUTPase inhibitor from blocking the B. subtilis dUTPase activity, thereby allowing the degradation of dUTP and the synthesis of dTTP (both of which are DNA polymerase substrates), so that thymine replaces some of the uracil normally found in PBS2 DNA. pbs2 Deoxyuridine triphosphatase Drosophila melanogaster
4 We propose that infection at high pH prevents the PBS2-induced dUTPase inhibitor from blocking the B. subtilis dUTPase activity, thereby allowing the degradation of dUTP and the synthesis of dTTP (both of which are DNA polymerase substrates), so that thymine replaces some of the uracil normally found in PBS2 DNA. pbs2 Deoxyuridine triphosphatase Drosophila melanogaster