Circular dichroism and electron microscopy of a core Y61F mutant of the F1 gene 5 single-stranded DNA-binding protein and theoretical analysis of CD spectra of four Tyr → Phe substitutions

Biochemistry

Volumn 37, Issue 20, 1998, Pages 7463-7477

  Thompson, Teresa M ^a   Mark, Barbara L ^a   Gray, Carla W ^a   Terwilliger, Thomas C ^b   Sreerama, Narasimha ^c   Woody, Robert W ^c   Gray, Donald M ^a  

^a UNIVERSITY OF TEXAS AT DALLAS   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c Department of Environmental and Radiological Health Sciences   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA BINDING PROTEIN; PHENYLALANINE; SINGLE STRANDED DNA; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; BACTERIOPHAGE; CIRCULAR DICHROISM; CONTROLLED STUDY; DNA PROTEIN COMPLEX; ELECTRON MICROSCOPY; IONIC STRENGTH; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; BINDING SITES; CIRCULAR DICHROISM; DNA, SINGLE-STRANDED; DNA, SUPERHELICAL; DNA-BINDING PROTEINS; INOVIRUS; MACROMOLECULAR SUBSTANCES; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; POLY A; PROTEIN FOLDING; SOLUTIONS; TITRIMETRY; TYROSINE; VIRAL PROTEINS;

BACTERIA (MICROORGANISMS); BACTERIAL VIRUS;

EID: 0032546534     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972545k     Document Type: Article

References (65)

1. Model, P., and Russell, M. (1988) in The Bacteriophages (Calendar, R. Ed.) pp 386-390, Plenum Press, New York.
2. Alberts, B., Frey, L., and Delius, H. (1972) J. Mol. Biol. 68, 139-152.
3. McPherson, A., Jurnak, F., Wang, A., Kopak, F., Molineux, I., and Rich, A. (1978) Cold Spring Harbor Symp. Quantum Biol. 43, 21-28.
4. Gray, C. W., Kneale, G. G., Leonard, K. R., Siegrist, H., and Marvin, D. A. (1982) Virology 116, 40-52.
5. Gray, C. W. (1989) J. Mol. Biol. 208, 57-64.
6. Olah, G. A., Gray, D. M., Gray, C. W., Kergil, D. L., Sosnick, T. R., Mark, B. L., Vaughan, M. R., and Trewhella, J. (1995) J. Mol. Biol. 249, 576-594.
7. Gray, D. M., Gray, C. W., and Carlson, R. D. (1982) Biochemistry 21, 2702-2713.
8. Skinner, M. M., Zhang, H., Leschnitzer, D. H., Guan, Y., Bellamy, H., Sweet, R. M., Gray, C. W., Konings, R. N. H., Wang, A. H.-J., and Terwilliger, T. C. (1994) Proc. Natl. Acad. Sci. U.S.A. 91, 2071-2075.
9. Murzin, A. G. (1993) EMBO J. 12, 861-867.
10. Ruff, M., Krishnaswamy, S., Boeglin, M., Poterzman, A., Mitschler, A., Podjarny, A., Rees, B., Thierry, J. C., and Moras, D. (1991) Science 252, 1682-1689.
11. Folmer, R. H. A., Nilges, M., Konings, R. N. H., and Hilbers, C. W. (1995) EMBO J. 14, 4132-4142.
12. Bochkarev, A., Pfuetzner, R. A., Edwards, A. M., and Frappier, L. (1997) Nature 385, 176-181.
13. van Duyenhoven, J. P. M., Folkers, P. J. M., Prinse, C. W. J. M., Harmsen, B. J. M., Konings, R. N. H., and Hilbers, C. W. (1992) Biochemistry 31, 1254-1262.
14. Peeters, B. P. H., Konings, R. N. H., and Schoenmakers, J. G. G. (1983) J. Mol. Biol. 169, 197-215.
15. King, G. C., and Coleman, J. E. (1987) Biochemistry 26, 2929-2937.
16. Folkers, P. J. M., Stassen, A. P. M., van Duynhoven, J. P. M., Harmsen, B. J. M., Konings, R. N. H., and Hilbers, C. W. (1991) Eur. J. Biochem. 200, 139-148.
17. King, G. C., and Coleman, J. E. (1988) Biochemistry 27, 6947-6953.
18. Stassen, A. P. M., Harmsen, B. J. M., Schoenmakers, J. G. G., Hilbers, C. W., and Konings, R. N. H. (1992) Eur. J. Biochem. 206, 605-612.
19. Guan, Y., Zhang, H., Konings, R. N. H., Hilbers, C. W., Terwilliger, T. C., and Wang, A. H.-J. (1994) Biochemistry 33, 7768-7778.
20. Mark, B. L., Terwilliger, T. C., Vaughan, M. R., and Gray, D. M. (1995) Biochemistry 34, 12854-12865.
21. Terwilliger, T. C., Zabin, H. B., Horvath, M. P., Sandberg, W. S., and Schlunk, P. M. (1994) J. Mol. Biol. 236, 556-571.
22. Stassen, A. P. M., Zaman, G. J. R., van Deursen, J. M. A., Schoenmakers, J. G. G., and Konings, R. N. H. (1992) Eur. J. Biochem. 204, 1003-1014.
23. Kansy, J. W., Clack, B. A., and Gray, D. M. (1986) J. Biomol. Struct. Dyn. 3, 1079-1110.
24. McGhee, J. D., and von Hippel, P. H. (1974) J. Mol. Biol. 86, 469-489.
25. Alma, N. C. M., Harmsen, B. J. M., de Jong, E. A. M., van der Ven, J., and Hilbers, C. W. (1983) J. Mol. Biol. 163, 47-62.
26. Bulsink, H., Harmsen, B. J. M., and Hilbers, C. W. (1988) Eur. J. Biochem. 176, 597-608.
27. Pratt, D., Laws, P., and Griffith, J. (1974) J. Mol. Biol. 82, 425-439.
28. Day, L. A. (1973) Biochemistry 12, 5329-5339.
29. Manning, M. C., and Woody, R. W. (1991) Biopolymers 31, 569-586.
30. Terwilliger, T. C. (1988) Gene 71, 41-47.
31. Anderson, R. A., Nakashima, Y., and Coleman, J. E. (1975) Biochemistry 14, 907-917.
32. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning, A Laboratory Manual, 2nd ed.; Vol. 3, pp 18.47-18.55. Cold Spring Harbor Laboratory Press.
33. Savitsky, A., and Golay, M. J. E. (1964) Anal. Chem. 36, 1627-1639.
34. Gray, C. W. (1994) in Methods in Molecular Biology, Vol. 30: DNA-Protein Interactions: Principles and Protocols (Kneale, G. G., Ed.) pp 347-356. Humana Press, NY.
35. Bayley, P. M., Nielsen, E. B., and Schellman, J. A. (1969) J. Phys. Chem 73, 228-243.
36. Goux, W. J., and Hooker, T. M. (1980) J. Am. Chem. Soc. 102, 7080-7087.
37. Moffitt, W. (1956) J. Chem. Phys. 25, 467-478.
38. Brown, A., Kemp, C. M., and Mason, S. F. (1971) J. Chem. Soc. A 751-755.
39. Neilsen, E. B., and Schellman, J. A. (1971) Biopolymers 10, 1559-1581.
40. Mandel, R., and Holzwarth, G. (1972) J. Chem. Phys. 57, 3469-3477.
41. Chen, Y. H., Yang, J. T., and Chan, K. H. (1974) Biochemistry 13, 3350-3359.
42. Yamaoka, K., Ueda, K., and Kosako, I. (1986) J. Am. Chem. Soc. 108, 4619-4625.
43. Weiner, S. J., Kollman, P. A., Case, D. A., Singh, U. C., Ghio, C., Algona, G., Profeta, S., Jr., and Weiner, P. (1984) J. Am. Chem. Soc. 106, 765-784.
44. Mark, B. L., and Gray, D. M. (1997) Biopolymers 42, 337-348.
45. Benevides, J. M., Terwilliger, T. C., Vohnik, S., and Thomas, G. J., Jr. (1996) Biochemistry 35, 9603-9609.
46. Record, M. T., Jr., Lohman, T. M., and de Haseth, P. (1976) J. Mol. Biol. 107, 145-158.
47. Terwilliger, T. C. (1996) Biochemistry 35, 16652-16664.
48. Beck, E., Sommer, R., Auerswald, E. A., Kurz, Ch., Zink, B., Osterburg, G., and Schaller, H. (1978) Nucleic Acids Res. 5, 4497-4503.
49. Gray, C. W. (1985) in Fourth Conversation in Biomolecular Stereodynamics (Sarma, R. H., Ed.) Adenine Press, NY, pp 219-220.
50. Haase-Pettingell, C. A., and King, J. (1988). J. Biol. Chem. 10, 4977-4983.
51. Yu, M.-H., and King, J. (1988) J. Biol. Chem. 263, 1424-1431.
52. Zabin, H. B., & Terwilliger, T. C. (1991) J. Mol. Biol. 219, 257-275.
53. Burley, S. K., and Petsko, G. A. (1985) Science 229, 23-28.
54. Johnson, W. C., Jr. (1996) in Circular Dichroism and the Conformational Analysis of Biomolecules (Fasman, G. D., Ed.), pp 433-468. Plenum Press, NY.
55. Scheerhagen, M. A., Bokma, J. T., Vlaanderen, C. A., Blok, J., and van Grondelle, R. (1986) Biopolymers 25, 1419-1448.
56. Pörschke, D., and Rauh, H. (1983) Biochemistry 22, 4737-4745.
57. Sang, B.-C., and Gray, D. M. (1989) J. Biomol. Struct. Dyn. 7, 693-706.
58. Shiraki, M. (1969) Sci. Papers, College Gen. Educ. (University Tokyo) 19, 151-173.
59. Durand, M., Maurizot, J.-C., Borazan, H. N., and Helène, C. (1975) Biochemistry 14, 563-570.
60. Strickland, E. H. (1974) CRC Crit. Rev. Biochem. 2, 113-175.
61. Woody, R. W. (1995) Methods Enzymol. 246, pp 34-41.
62. Liang, H., and Terwilliger, T. C. (1991) Biochemistry 30, 2772-2782.
63. Koslowski, A, Botterweck, H., Fleischhauer, J., Kurapkat, G., Wollmer, A., and Woody, R. W. (1996) Prog. Biophys. Mol Biol. 65, Suppl. 1, 43.
64. Grishina, I. B., and Woody, R. W. (1994) Faraday Discuss. 99, 245-262.
65. Kurapkat, G., Krüger, P., Wollmer, A., Fleischhauer, J., Kramer, B., Zobel, E., Koslowski, A, Botterweck, H., and Woody, R. W. (1996) Biopolymers 41, 267-287.