Disease relevance of T7p10

• Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7 [1].
• The 350 amino acid catalytic core of the vaccinia ligase is similar in size and protease-sensitivity to the full-length bacteriophage T7 DNA ligase [2].
• Thermus thermophilus (Tth) DNA ligase is unable to join any oligonucleotide of length six or less, while T4 DNA ligase and T7 DNA ligase are both able to join hexamers [3].
• Expression of the unassembled capsid protein during infection of Shigella sonnei by bacteriophage T7 results in DNA damage that is repairable by bacteriophage T3, but not T7, DNA ligase [4].

High impact information on T7p10

• Chlorella virus DNA ligase is the smallest eukaryotic ATP-dependent ligase known; it has an intrinsic nick-sensing function and suffices for yeast cell growth [5].
• DNA synthesis catalyzed by Form II of T7 DNA polymerase eliminates gaps to create a substrate for DNA ligase whereas strand displacement synthesis catalyzed by Form I creates an aberrant structure that cannot be joined [6].
• The requirement for Watson-Crick base pairing surrounding a nick in duplex DNA to be sealed by DNA ligase is the basis for oligonucleotide ligation assays that distinguish single base mutations in DNA targets [3].
• Recombination was found to be independent of DNA ligase and DNA packaging and maturation functions [7].

Analytical, diagnostic and therapeutic context of T7p10

• Bacteriophage T7 DNA ligase. Overexpression, purification, crystallization, and characterization [8].
• The rate of oligonucleotide ligation by Tth DNA ligase increases between heptamer and nonamer [3].

References