Mycobacterial Ku and ligase proteins constitute a two-component NHEJ repair machine

Science

Volumn 306, Issue 5696, 2004, Pages 683-685

  Della, Marina ^a,f   Palmbos, Phillip L ^b   Tseng, Hui Min ^c   Tonkin, Louise M ^a,d   Daley, James M ^b   Topper, Leana M ^b   Pitcher, Robert S ^d   Tomkinson, Alan E ^e   Wilson, Thomas E ^b   Doherty, Aidan J ^d  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^c UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

^d UNIVERSITY OF SUSSEX   (United Kingdom)

^e UNIVERSITY OF MARYLAND SCHOOL OF MEDICINE   (United States)

^f INSTITUTE OF CANCER RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; DNA; GENES; KURCHATOVIUM; YEAST;

DOUBLE-STRAND BREAKS (DSB); END-PROCESSING REACTIONS; MAMMALIAN CELLS; NONHOMOLOGOUS END-JOINING (NHEJ);

ENZYMES;

BACTERIAL PROTEIN; DEOXYRIBONUCLEASE; DNA LIGASE D; DNA POLYMERASE; KU ANTIGEN; LIGASE; PHOSPHODIESTERASE I; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; UNCLASSIFIED DRUG;

DNA;

ARTICLE; BACTERIAL GENOME; DNA REPAIR; DNA STRAND BREAKAGE; ENZYME ACTIVITY; IN VITRO STUDY; MYCOBACTERIUM TUBERCULOSIS; NONHOMOLOGOUS END JOINING SYSTEM; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROCESSING; SEQUENCE HOMOLOGY;

BACTERIAL PROTEINS; DNA; DNA DAMAGE; DNA LIGASES; DNA NUCLEOTIDYLTRANSFERASES; DNA PRIMASE; DNA REPAIR; DNA-DIRECTED DNA POLYMERASE; EXONUCLEASES; MUTATION; MYCOBACTERIUM TUBERCULOSIS; POLYMERASE CHAIN REACTION; PROTEIN STRUCTURE, TERTIARY; RECOMBINATION, GENETIC; SACCHAROMYCES CEREVISIAE;

BACTERIA (MICROORGANISMS); MAMMALIA; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; PROKARYOTA;

EID: 7444269607     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1099824     Document Type: Article

References (30)

1. L. Krejci, L. Chen, S. Van Komen, P. Sung, A. E. Tomkinson, Prog. Nucleic Acid Res. Mol. Biol. 74, 159 (2003).
2. S. E. Critchlow, S. P. Jackson, Trends Biochem. Sci. 23, 394 (1998).
3. G. R. Weller et al., Science 297, 1686 (2002).
4. L. G. DeFazio, R. M. Stansel, J. D. Griffith, G. Chu, EMBO J. 21, 3192 (2002).
5. D. Ramsden, M. Gellert, EMBO J. 17, 609 (1998).
6. L. Chen, K. Trujillo, W. Ramos, P. Sung, A. E. Tomkinson, Mol. Cell 8, 1105 (2001).
7. L. Chen, K. Trujillo, P. Sung, A. E. Tomkinson, J. Biol. Chem. 275, 26196 (2000).
8. S. A. Nick McElhinny, C. M. Snowden, J. McCarville, D. Ramsden, Mol. Cell. Biol. 20, 2996 (2000).
9. L. Aravind, E. V. Koonin, Genome Res. 11, 1365 (2001).
10. E. V. Koonin, Y. I. Wolf, A. S. Kondrashov, L. Aravind, J. Mol. Microbiol. Biotechnol. 2, 509 (2000).
11. G. R. Weller, A. J. Doherty, FEBS Lett. 505, 340 (2001).
12. T. E. Wilson, L. M. Topper, P. L. Palmbos, Trends Biochem. Sci. 28, 62 (2003).
13. B. Arezi, R. Kuchta, Trends Biochem. Sci. 11, 572 (2000).
14. K. N. Mahajan, S. A. Nick McElhinney, B. S. Mitchell, D. A. Ramsden, Mol. Cell. Biol. 22, 5194 (2002).
15. H.-M. Tseng, A. E. Tomkinson, J. Biol. Chem. 277, 45630 (2002).
16. T. E. Wilson, M. R. Lieber, J. Biol. Chem. 274, 23599 (1999).
17. S. A. Nick McElhinney, D. Ramsden, Mol. Cell. Biol. 23, 2309 (2003).
18. M. Della et al., unpublished data.
19. D. A. Ramsden, T. T. Paull, M. Gellert, Nature 388, 488 (1997).
20. E. Karathanasis, T. E. Wilson, Genetics 161, 1015 (2002).
21. T. E. Wilson, Genetics 162, 677 (2002).
22. S. J. Boulton, S. P. Jackson, EMBO J. 17, 1819 (1998).
23. J. C. Connelly, D. R. Leach, Trends Biochem. Sci. 27, 410 (2002).
24. T. E. Wilson, U. Grawunder, M. R. Lieber, Nature 388, 495 (1997).
25. J. K. Moore, J. E. Haber, Mol. Cell. Biol. 16, 2164 (1996).
26. K. Bebenek, M. Garcia-Diaz, L. Blanco, T. A. Kunkel, J. Biol. Chem. 278, 34685 (2003).
27. M. Garcia-Diaz et al., Mol. Cell 13, 561 (2004).
28. S. Covo, L. Blanco, Z. Livneh, J. Biol. Chem. 279, 859 (2004).
29. B. Rydberg, J. Game, Proc. Natl. Acad. Sci. U.S.A. 99, 16654 (2002).
30. We thank S. Bell and E. Koonin for discussions, S. Bell for assistance with assays, and T. Carr, P. Jeggo, and K. Caldecott for comments on the manuscript. A.J.D. is a Royal Society University Research Fellow and L.T. is supported by a Biotechnology and Biological Sciences Research Council (BBSRC) studentship. Supported by grants from the BBSRC, the Association for International Cancer Research, the Royal Society, the U.S. Public Health Service, and the Pew Charitable Trusts. Molecular interaction data have been deposited in the Biomolecular Interaction Network Database with accession code 153967.