DNA ligases in the repair and replication of DNA

• Published in: Mutation research Vol. 460; no. 3-4; pp. 301 - 318
• Main Authors: Timson, David J, Singleton, Martin R, Wigley, Dale B
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 30.08.2000
• Subjects: Adenosine Triphosphate - physiology; Adult; Allosteric Regulation; Amino Acid Sequence; Archaeal Proteins - chemistry; Archaeal Proteins - metabolism; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Binding Sites; BRCT domain; Catalysis; DNA - chemistry; DNA - metabolism; DNA ligase; DNA Ligase ATP; DNA Ligases - chemistry; DNA Ligases - physiology; DNA Repair; DNA Replication; Eukaryotic Cells - enzymology; Genetic Diseases, Inborn - genetics; Humans; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NAD - physiology; Non-homologous end joining; Okazaki fragment; Poly-ADP-Ribose Binding Proteins; Prokaryotic Cells - enzymology; Protein Conformation; Protein Isoforms - chemistry; Protein Isoforms - physiology; Protein structure; Protein Structure, Tertiary; Radiation Tolerance - genetics; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity; Structure-Activity Relationship; V(D)J recombination; Viral Proteins - chemistry; Viral Proteins - metabolism; Xenopus Proteins; BRCT domain; Protein structure; DNA repair; V(D)J recombination; Non-homologous end joining; Okazaki fragment

DNA ligases are critical enzymes of DNA metabolism. The reaction they catalyse (the joining of nicked DNA) is required in DNA replication and in DNA repair pathways that require the re-synthesis of DNA. Most organisms express DNA ligases powered by ATP, but eubacteria appear to be unique in having l...