Structure of RecJ exonuclease defines its specificity for single-stranded DNA

Journal of Biological Chemistry

Volumn 285, Issue 13, 2010, Pages 9762-9769

  Wakamatsu, Taisuke ^a   Kitamura, Yoshiaki ^b   Kotera, Yutaro ^a   Nakagawa, Noriko ^a,b   Kuramitsu, Seiki ^a,b   Masui, Ryoji ^a,b  

^a OSAKA UNIVERSITY   (Japan)

^b Harima Institute ^*  (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

DNA REPAIR; EXONUCLEASE; HIGH SPECIFICITY; HYDROLYSIS REACTION; LIGAND-FREE; SINGLE-STRANDED DNA; SINGLE-STRANDED DNA (SS-DNA); SPECIFIC BINDING; STRUCTURAL FEATURE; STRUCTURAL SIMILARITY;

DNA; GENES; MANGANESE; MANGANESE COMPOUNDS; METAL IONS;

X RAY CRYSTALLOGRAPHY;

MAGNESIUM ION; MANGANESE; OLIGONUCLEOTIDE; OLIGOSACCHARIDE; RECJ PROTEIN; SINGLE STRANDED DNA; BACTERIAL PROTEIN; EXODEOXYRIBONUCLEASE; ION; MAGNESIUM; RECJ PROTEIN, BACTERIA;

ARTICLE; BINDING AFFINITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; STRUCTURAL HOMOLOGY; X RAY CRYSTALLOGRAPHY; CHEMICAL STRUCTURE; CHEMISTRY; ENZYMOLOGY; GENETICS; KINETICS; METHODOLOGY; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; THERMUS THERMOPHILUS;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DNA, SINGLE-STRANDED; EXODEOXYRIBONUCLEASES; HYDROLYSIS; IONS; KINETICS; MAGNESIUM; MANGANESE; MODELS, MOLECULAR; OLIGONUCLEOTIDES; OLIGOSACCHARIDES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; THERMUS THERMOPHILUS;

EID: 77951231950     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.096487     Document Type: Article

References (34)

1. Lovett, S. T., and Clark, A. J. (1984) J. Bacteriol. 157, 190-196
2. Handa, N., Morimatsu, K., Lovett, S. T., and Kowalczykowski, S. C. (2009) Genes Dev. 23, 1234-1245
3. Burdett, V., Baitinger, C., Viswanathan, M., Lovett, S. T., and Modrich, P. (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 6765-6770
4. Viswanathan, M., Burdett, V., Baitinger, C., Modrich, P., and Lovett, S. T. (2001) J. Biol. Chem. 276, 31053-31058
5. Dianov, G., Sedgwick, B., Daly, G., Olsson, M., Lovett, S., and Lindahl, T. (1994) Nucleic Acids Res. 22, 993-998
6. Rajman, L. A., and Lovett, S. T. (2000) J. Bacteriol. 182, 607-612
7. Lovett, S. T., and Kolodner, R. D. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 2627-2631
8. Sharma, R., and Rao, D. N. (2009) J. Mol. Biol. 385, 1375-1396
9. Han, E. S., Cooper, D. L., Persky, N. S., Sutera, V. A., Jr., Whitaker, R. D., Montello, M. L., and Lovett, S. T. (2006) Nucleic Acids Res. 34, 1084-1091
10. Yamagata, A., Kakuta, Y., Masui, R., and Fukuyama, K. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 5908-5912
11. Aravind, L., and Koonin, E. V. (1998) Trends Biochem. Sci. 23, 17-19
12. Kuramitsu, S., Hiromi, K., Hayashi, H., Morino, Y., and Kagamiyama, H. (1990) Biochemistry 29, 5469-5476
13. Yamagata, A., Masui, R., Kakuta, Y., Kuramitsu, S., and Fukuyama, K. (2001) Nucleic Acids Res. 29, 4617-4624
14. Otwinowski, Z., and Minor, W. (1997) Methods Enzymol. 276, 307-326
15. Matthews, B. W. (1968) J. Mol. Biol. 33, 491-497
16. Vagin, A., and Teplyakov, A. (1997) J. Appl. Crystallogr. 30, 1022-1025
17. Adams, P. D., Grosse-Kunstleve, R. W., Hung, L. W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., and Terwilliger, T. C. (2002) Acta Crystallogr. D Biol. Crystallogr. 58, 1948-1954
18. Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Acta Crystallogr. Sect. A 47, 110-119
19. Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998) Acta Crystallogr. D Biol. Crystallogr. 54, 905-921
20. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., 3rd, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) Nucleic Acids Res. 35, W375-W383
21. Collaborative Computational Project, Number 4 (1994) Acta Crystallogr. D Biol. Crystallogr. 50, 760-763
22. Murzin, A. G. (1993) EMBO J. 12, 861-867
23. Leiros, I., Timmins, J., Hall, D. R., and McSweeney, S. (2005) EMBO J. 24, 906-918
24. Theobald, D. L., Mitton-Fry, R. M., and Wuttke, D. S. (2003) Annu. Rev. Biophys. Biomol. Struct. 32, 115-133
25. Bochkarev, A., and Bochkareva, E. (2004) Curr. Opin. Struct. Biol. 14, 36-42
26. Beese, L. S., and Steitz, T. A. (1991) EMBO J. 10, 25-33
27. Ugochukwu, E., Lovering, A. L., Mather, O. C., Young, T. W., and White, S. A. (2007) J. Mol. Biol. 371, 1007-1021
28. Kovall, R. A., and Matthews, B. W. (1999) Curr. Opin. Chem. Biol. 3, 578-583
29. Nowotny, M., Gaidamakov, S. A., Crouch, R. J., and Yang, W. (2005) Cell 121, 1005-1016
30. Sutera, V. A., Jr., Han, E. S., Rajman, L. A., and Lovett, S. T. (1999) J. Bacteriol. 181, 6098-6102
31. Schubert, M., Edge, R. E., Lario, P., Cook, M. A., Strynadka, N. C., Mackie, G. A., and McIntosh, L. P. (2004) J. Mol. Biol. 341, 37-54
32. Zuo, Y., Vincent, H. A., Zhang, J., Wang, Y., Deutscher, M. P., and Malhotra, A. (2006) Mol. Cell 24, 149-156
33. Lorentzen, E., Basquin, J., Tomecki, R., Dziembowski, A., and Conti, E. (2008) Mol. Cell 29, 717-728
34. Meier, B., Barber, L. J., Liu, Y., Shtessel, L., Boulton, S. J., Gartner, A., and Ahmed, S. (2009) EMBO J. 28, 3549-3563