Disease relevance of pol

• The highly processive DNA polymerase of bacteriophage T5. Role of the unique N and C termini [1].
• With "nicked DNA-like" poly(dA):oligo(dT), the processiveness of E. coli DNA polymerase I is increased 2- to 2.5-fold [2].

High impact information on pol

• Further, amino acid sequence comparisons of T5 DNA polymerase with a large group of DNA polymerases previously shown to exhibit little similarity to polymerase I indicate certain sequence segments are shared among distantly related DNA polymerases [3].
• Although T5 DNA polymerase shares extensive sequence homology with Escherichia coli DNA polymerase I and T7 DNA polymerase, it contains unique regions of 130 and 71 residues at its N and C termini, respectively [1].
• The 5' nuclease of DNA polymerase I (Pol I) of Escherichia coli is a member of an important class of prokaryotic and eukaryotic nucleases, involved in DNA replication and repair, with specificity for the junction between single-stranded and duplex DNA [4].
• Properties of overexpressed phage T5 D15 exonuclease. Similarities with Escherichia coli DNA polymerase I 5'-3' exonuclease [5].
• Using this procedure, we have found that Escherichia coli DNA polymerase I, T4 DNA polymerase, and calf thymus alpha- and beta-DNA polymerase are "quasi-processive." Most of these enzymes add on the average approximately 10 to 15 nucleotides before dissociating from the template [2].

Chemical compound and disease context of pol

• 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 [6].

Biological context of pol

• Because the structural gene for T5 DNA polymerase is estimated to be 2,600 base pairs long, the whole structural gene may reside in these segments [7].
• T5 DNA polymerase (T5Pol), an essential enzyme for bacteriophage T5 DNA replication, is unusual because of its high processivity and strand-displacing ability [8].
• The 3' leads to 5' exonuclease associated with T5 DNA polymerase was not very active with nicked DNA, but inhibition of hydrolysis of substituents at 3'-hydroxyl termini by gpD5 could be observed [9].

Other interactions of pol

• Interaction of a DNA-binding protein, the product of gene D5 of bacteriophage T5, with double-stranded DNA: effects on T5 DNA polymerase functions in vitro [9].

References