Amino acid substitutions at position 43 of NaeI endonuclease: Evidence for changes in NaeI structure

Journal of Biological Chemistry

Volumn 278, Issue 11, 2003, Pages 9733-9739

  Carrick, Kevin L ^b   Topal, Michael D ^a  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENZYMES; MOLECULAR STRUCTURE; SUBSTITUTION REACTIONS;

PROTEOLYSIS;

AMINO ACIDS;

ALANINE; AMINO ACID; AMSACRINE; ARGININE; ASPARAGINE; DNA; DNA TOPOISOMERASE; ENDONUCLEASE; GLUTAMIC ACID; HISTIDINE; LEUCINE; LIGASE; LYSINE; NAEI ENDONUCLEASE; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; RECOMBINASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; ENDODEOXYRIBONUCLEASE NAEI; PROTEIN; RESTRICTION ENDONUCLEASE; TYPE II SITE SPECIFIC DEOXYRIBONUCLEASE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CIRCULAR DICHROISM; DNA BINDING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; MELTING POINT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; ULTRAVIOLET SPECTROSCOPY; CHEMICAL STRUCTURE; CHEMISTRY; CHROMATOGRAPHY; DIMERIZATION; DOSE RESPONSE; ENZYMOLOGY; ESCHERICHIA COLI; METABOLISM; MOLECULAR GENETICS; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MOTIF; SEQUENCE HOMOLOGY; TEMPERATURE; ULTRAVIOLET RADIATION; X RAY CRYSTALLOGRAPHY;

ANIMALIA;

ALANINE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; AMINO ACIDS; ASPARAGINE; CHROMATOGRAPHY; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; DEOXYRIBONUCLEASES, TYPE II SITE-SPECIFIC; DIMERIZATION; DNA LIGASES; DNA RESTRICTION ENZYMES; DNA TOPOISOMERASES; DOSE-RESPONSE RELATIONSHIP, DRUG; ESCHERICHIA COLI; GLUTAMIC ACID; HISTIDINE; LEUCINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE; ULTRAVIOLET RAYS;

EID: 0037984366     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M209192200     Document Type: Article

References (35)

1. Oller, A. R., Vanden Broek, W., Conrad, M., and Topal, M. D. (1991) Biochemistry 30, 2543-2549
2. Reuter, M., Kupper, D., Pein, C.-D., Petrusyte, M., Siksnys, V., Frey, B., and Krüger, D. (1993) Anal. Biochem. 209, 232-237
3. Yang, C. C., Baxter, B. K., and Topal, M. D. (1994) Biochemistry 33, 14918-14925
4. Conrad, M., and Topal, M. D. (1989) Proc. Nat. Acad. Sci. U. S. A. 86, 9707-9711
5. Topal, M. D., Thresher, R. J., Conrad, M., and Griffith, J. (1991) Biochemistry 30, 2006-2010
6. Yang, C. C., and Topal, M. D. (1992) Biochemistry 31, 9657-9664
7. Baxter, B. K., and Topal, M. D. (1993) Biochemistry 32, 8291-8298
8. Holtz, J. K., and Topal, M. D. (1994) J. Biol. Chem. 269, 27286-27290
9. Taron, C. H., Van Cott, E. M., Wilson, G. G., Moran, L. S., Slatko, B. E., Hornstra, L. J., Benner, J. S., Kucera, R. B., and Guthrie, E. P. (1995) Gene (Amst.) 155, 19-25
10. Jo, K., and Topal, M. D. (1995) Science 267, 1817-1820
11. Jo, K., and Topal, M. D. (1996) Biochemistry 35, 10014-10018
12. Jo, K., and Topal, M. D. (1996) Nucleic Acids Res. 24, 4171-4175
13. Huai, Q., Colandene, J. D., Chen, Y., Luo, F., Zhao, Y., Topal, M. D., and Ke, H. (2000) EMBO J. 19, 3110-3118
14. Huai, Q., Colandene, J. D., Topal, M. D., and Ke, H. (2001) Nat. Struct. Biol. 8, 665-669
15. Ban, C., and Yang, W. (1998) EMBO J. 17, 1526-1534
16. Tsutakawa, S. E., Muto, T., Kawate, T., Jingami, H., Kunishima, N., Ariyoshi, M., Kohda, D., Nakagawa, M., and Morikawa, K. (1999) Mol. Cell 3, 621-628
17. Kovall, R. A., and Matthews, B. W. (1999) Curr. Opin. Chem. Biol. 3, 578-583
18. Hickman, A. B., Li, Y., Mathew, S. V., May, E. W., Craig, N. L., and Dyda, F. (2000) Mol. Cell 5, 1025-1034
19. Berger, J. M., Fass, D., Wang, J. C., and Harrison, S. C. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 7876-7881
20. Shuman, S., and Schwer, B. (1995) Mol. Microbiol. 17, 405-410
21. Subramanya, H. S., Doherty, A. J., Ashford, S. R., and Wigley, D. B. (1996) Cell 85, 607-615
22. Singleton, M. R., Håkansson, K., Timson, D. J., and Wigley, D. B. (1999) Structure 7, 35-42
23. Lee, J. Y., Chang, C., Song, H. K., Moon, J., Yang, J. K., Kim, H.-K., Kwon, S.-T., and Suh, S. W. (2000) EMBO J. 19, 1119-1129
24. Odell, M., Sriskanda, V., Shuman, S., and Nikolov, D. B. (2000) Mol. Cell 6, 1183-1193
25. Clackson, T., Gussow, D., and Jones, P. T. (1991) in PCR-A Practical Approach (Quirke, P., and Taylor, G. R., eds) pp. 187-214, Oxford University Press, New York
26. Jo, K., and Topal, M. D. (1998) Nucleic Acids Res. 26, 2380-2384
27. Colandene, J. D., and Topal, M. D. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 3531-3536
28. Provencher, S. W., and Glockner, J. (1981) Biochemistry 20, 33-37
29. Sriskanda, V. Schwer, B., Ho, C. K., and Shuman, S. (1999) Nucleic Acids Res. 27, 3953-3963
30. Dayhoff, M. O., Schwartz, R. M., and Orcott, B. L. (1978) in Atlas of Protein Sequence and Structure (Dayhoff, M. O., ed) Vol. 5, Suppl. 3, pp. 345-352, National Biomedical Research Foundation, Washington, D. C.
31. Cantor, C. R., and Schimmel, P. R. (1980) Biophysical Chemistry, Part II: Techniques for the study of biological structure and function, pp. 425-428, W. H. Freeman and Co., San Francisco, CA
32. Sriskanda, V., and Shuman, S. (2002) Nucleic Acids Res. 30, 903-911
33. Cong, P., and Shuman, S. J. (1993) J. Biol. Chem. 268, 7256-7260
34. Heaphy, S., Singh, M., and Gait, M. J. (1987) Biochemistry 26, 1688-1696
35. Sriskanda, V., and Shuman, S. (1998) Nucleic Acids Res. 26, 4618-4625