DNA ligase: Difference between revisions
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<StructureSection load='2hix' size='400' side='right' scene='DNA_ligase/Cv/1' caption='ATP-dependent DNA ligase complexed with ATP [[2hix]]'> | <StructureSection load='2hix' size='400' side='right' scene='DNA_ligase/Cv/1' caption='ATP-dependent DNA ligase complexed with ATP [[2hix]]'> | ||
'''DNA ligase''' (LigD) is an enzyme which repairs single-stranded breaks in a double-stranded DNA. LigD is activated , in a species-dependent manner, by hydrolysis of ATP or NAD+. | '''DNA ligase''' (LigD) is an enzyme which repairs single-stranded breaks in a double-stranded DNA. LigD is activated, in a species-dependent manner, by hydrolysis of ATP or NAD+.<br /> | ||
* Mammalian '''LigD I''' ligates the nascent DNA of the lagging strand.<br /> | |||
* '''LigD III''' complexes with XRCC1 in the process of nucleotide excision repair.<br /> | |||
* '''LigD IV''' complexes with XRCC4 and catalyzes the last step in the non-homologous DNA end joining.<br /> | |||
See more details in [[ATP-Dependent DNA Ligase (Bacteriophage T7)]]. | |||
==Disease== | ==Disease== | ||
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A specific point mutation (46BR in the mouse Lig1 gene) in DNA ligase I has also been linked as a cause for genome instability and cancer in humans. One possible reason for this is the accumulation of DNA fragments that are no longer ligated by the mutant DNA ligase I enzyme. | A specific point mutation (46BR in the mouse Lig1 gene) in DNA ligase I has also been linked as a cause for genome instability and cancer in humans. One possible reason for this is the accumulation of DNA fragments that are no longer ligated by the mutant DNA ligase I enzyme. | ||
== Structural highlights == | |||
LigD contains several domains: adenylation domain; DNA-binding domain and the ca. 100 amino acid long BRCT motif. | |||
</StructureSection> | </StructureSection> | ||