Disease relevance of lig

• In this paper we describe two new types of phage mutants for the Mu lig function [1].
• When DNA ligase seals this nick, the product is a highly negatively superhelical molecule that can be relaxed by E. coli topoisomerase I. This unwinding requires a high degree of homology since phi X174 single-stranded DNA does not serve as a cofactor in the unwinding of G4 DNA, even though these molecules are 70% homologous [2].
• Limited proteolysis of the NAD+-dependent DNA ligase from Bacillus stearothermophilus with thermolysin results in two fragments which were resistant to further proteolysis [3].
• Cloning and functional characterization of an NAD(+)-dependent DNA ligase from Staphylococcus aureus [4].
• Plasmid containing a DNA ligase gene from Haemophilus influenzae [5].

High impact information on lig

• Second, synthetic DNA corresponding to the specific binding site is catenated extensively using DNA ligase [6].
• These data suggest that DNA ligase I is negatively regulated by its N-terminal region and that this inhibition can be relieved by post-translational modification [7].
• Circularization achieved with DNA ligase, followed by linearization at random with DNase I, and incorporation of the linearized, repaired, blunt-ended, rearranged genes into a suitable plasmid permitted the expression of randomly permuted polypeptide chains [8].
• The DNA ligase was purified to near-homogeneity by the two-step column chromatographic procedure from BLphLig-I cells that had been induced with isopropyl beta-D-thiogalactoside [9].
• Role of the DNA ligase III zinc finger in polynucleotide binding and ligation [10].

Chemical compound and disease context of lig

• Orthologues of the putative S. aureus NAD(+)-dependent DNA ligase could be identified in the genomes of Bacillus stearothermophilus and other gram-positive bacteria and confirmed the presence of four conserved amino acid motifs, including motif I, KXDG with lysine 112, which is believed to be the proposed site of adenylation [4].
• Second-strand DNA was synthesized by employing the replacement synthesis method using Escherichia coli RNase H, E. coli DNA polymerase I, E. coli DNA ligase, and beta-NAD+ [11].

Biological context of lig

• Disruption of the putative zinc finger did not affect DNA ligase III activity on nicked DNA duplex, nor did it abolish DNA ligase III-alpha activity during DNA base excision repair in a cell-free assay [10].
• Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli [12].

Associations of lig with chemical compounds

• The Mu ligts mutants are conditional lethals defective for both integration and replication of DNA, unable to 'complement' the bacterial lig mutation; the map between B and lys [1].
• These results suggest that the putative zinc finger does not stimulate DNA ligase III activity on simple nicked DNA substrates, but indicate that this motif can target the binding and activity of DNA ligase III to nicked RNA homopolymer [10].
• It is thought that bisulfite acts to inhibit excision repair, perhaps by effects on DNA polymerase I, or DNA ligase [13].

Analytical, diagnostic and therapeutic context of lig

• Southern blot analysis indicated the conservation of the lig genes among pathogenic leptospires [14].
• Murine RBP-J kappa protein purified by J kappa-RS affinity chromatography did not show DNA cleavage activities but contained a strong DNA ligase activity [15].

References