LigD explained
| Multifunctional non-homologous end joining protein LigD |
| Symbol: | ligD |
| Organism: | Mycolicibacterium smegmatis ATCC 700084 |
| Uniprot: | A0R3R7 |
LigD is a multifunctional ligase/polymerase/nuclease (3'-phosphoesterase) found in bacterial non-homologous end joining (NHEJ) DNA repair systems.[1] It is much more error-prone than the more complex eukaryotic system of NHEJ, which uses multiple enzymes to fill its role.[2] The polymerase preferentially use rNTPs (RNA nucleotides), possibly advantageous in dormant cells.[3]
The actual architecture of LigD is variable.
- The LigD homolog in Bacillus subtilis does not have the nuclease domain.
- LigD with its ligase domain artificially removed can perform its function (with loss of fidelity) with a separate LigC acting as the ligase.[2]
- The LigD homolog in the archaeon Methanocella paludicola is broken into three single-domain proteins sharing an operon.[4]
Notes and References
- Della M, Palmbos PL, Tseng HM, etal . Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine . Science . 306 . 5696 . 683–5 . October 2004 . 15499016 . 10.1126/science.1099824 . 2004Sci...306..683D . 38823696 .
- Gong C, Bongiorno P, Martins A, etal . Mechanism of nonhomologous end-joining in mycobacteria: a low-fidelity repair system driven by Ku, ligase D and ligase C . Nat. Struct. Mol. Biol. . 12 . 4 . 304–12 . April 2005 . 15778718 . 10.1038/nsmb915 . 6879518 .
- Pitcher RS, Green AJ, Brzostek A, Korycka-Machala M, Dziadek J, Doherty AJ . NHEJ protects mycobacteria in stationary phase against the harmful effects of desiccation . DNA Repair (Amst.) . 6 . 9 . 1271–6 . September 2007 . 17360246 . 10.1016/j.dnarep.2007.02.009 .
- Bartlett . EJ . Brissett . NC . Doherty . AJ . Ribonucleolytic resection is required for repair of strand displaced nonhomologous end-joining intermediates. . Proceedings of the National Academy of Sciences of the United States of America . 28 May 2013 . 110 . 22 . E1984-91 . 10.1073/pnas.1302616110. 3670387 . 23671117 . 2013PNAS..110E1984B . free.
