Aromatic Amino Acids are Critical for Stability of the Bicoid Homeodomain

Journal of Biological Chemistry

Volumn 276, Issue 24, 2001, Pages 21506-21511

  Subramaniam, Vinod ^a   Jovin, Thomas M ^a   Rivera Pomar, Rolando V ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACIDS; DNA; MUTAGENESIS; PROTEINS; QUENCHING; RNA; SPECTROSCOPIC ANALYSIS;

HOMEODOMAIN (HD);

BIOCHEMISTRY;

AROMATIC AMINO ACID; HOMEODOMAIN PROTEIN; INITIATION FACTOR; NUCLEIC ACID BINDING PROTEIN; TRYPTOPHAN; AMINO ACID; BICOID PROTEIN, DROSOPHILA; INSECT PROTEIN; RECOMBINANT PROTEIN; TRANSACTIVATOR PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DNA HELIX; DROSOPHILA; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DNA INTERACTION; PROTEIN DOMAIN; PROTEIN STABILITY; RNA BINDING; SITE DIRECTED MUTAGENESIS; TRANSLATION REGULATION; AMINO ACID SUBSTITUTION; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; HEAT; METABOLISM; PROTEIN CONFORMATION; SPECTROFLUOROMETRY; THERMODYNAMICS;

AMINO ACID SUBSTITUTION; AMINO ACIDS, CYCLIC; ANIMALS; BINDING SITES; CIRCULAR DICHROISM; DROSOPHILA; HEAT; HOMEODOMAIN PROTEINS; INSECT PROTEINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS; TRANS-ACTIVATORS; TRYPTOPHAN;

EID: 0035877733     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M102292200     Document Type: Article

References (45)

1. Billeter, M. (1996) Prog. Biophys. Mol. Biol. 66, 211-225
2. Gehring, W. J., Affolter, M., and Burglin, T. (1994) Annu. Rev. Biochem. 63, 487-526
3. Dubnau, J., and Struhl, G. (1996) Nature 379, 694-699
4. Chan, S. K., and Struhl, G. (1997) Nature 388, 634
5. Rivera-Pomar, R., Niessing, D., Schmidt-Ott, U. Gehring, W. J., and Jäckle, H. (1996) Nature 379, 746-749
6. Driever, W., and Nüsslein-Volhard, C. (1988) Cell 54, 95-104
7. Burz, D., Rivera-Pomar, R., Jäckle, H., and Hanes, S. (1998) EMBO J. 17, 5998-6009
8. Rivera-Pomar, R., Lu, X., Perrimon, N., Taubert, H., and Jäckle, H. (1995) Nature 376, 253-256
9. Billeter, M., Qian, Y., Otting, G., Muller, M., Gehring, W. J., and Wuthrich, K. (1990) J. Mol. Biol. 214, 183-197
10. Qian, Y. Q., Billeter, M., Otting, G., Muller, M., Gehring, W. J., and Wuthrich, K. (1989) Cell 59, 573-580
11. Hirsch, J. A., and Aggarwal, A. K. (1995) EMBO J. 14, 6280-6291
12. Kissinger, C. R., Liu, B., Martin-Blanco, E.; Kornberg, T. B., and Pabo, C. O. (1990) Cell 63, 579-590
13. Otting, G., Qian, Y. Q., Billeter, M., Muller, M., Affolter, M., Gehring, W. J., and Wuthrich, K. (1990) EMBO J. 9, 3085-3092
14. Wolberger, C., Vershon, A. K., Liu, B., Johnson, A. D., and Pabo, C. O. (1991) Cell 67, 517-528
15. Tucker-Kellogg, L., Rould, M. A., Chambers, K. A., Ades, S. E., Sauer, R. T., and Pabo, C. O. (1997) Structure 5, 1047-1054
16. Gehring, W. J., Qian, Y. Q., Billeter, M., Furukubo-Tokunaga, K., Schier, A. F., Resendez-Perez, D., Affolter, M., Otting, G., and Wuthrich, K. (1994) Cell 78, 211-223
17. Treisman, J., Gonczy, P., Vashishtha, M., Harris, E., and Desplan, C. (1989) Cell 59, 553-562
18. Hanes, S., and Brent, R. (1989) Cell 57, 1275-1283
19. Hanes, S. D., Riddihough, G., Ish-Horowicz, D., and Brent, R. (1994) Mol. Cell. Biol. 14, 3364-3375
20. Schier, A. F., and Gehring, W. J. (1992) Nature 356, 804-807
21. Ades, S. E., and Sauer, R. T. (1994) Biochemistry 33, 9187-9194
22. Subramaniam, V., Rivera-Pomar, R., and Jovin, T. M. (1999) Biophys. J. 76, A108
23. Nanda, V. & Brand, L. (2000) Proteins Struct. Funct. Genet. 40, 112-125
24. Nanda, V., and Brand, L. (1999) Biophys. J. 76, A448
25. Yang, J. T., Wu, C.-S. C., and Martinez, H. M. (1986) Methods Enzymol. 130, 208-269
26. Morgan, C. G., Mitchell, A. C., Peacock, N., and Murray, J. G. (1995) Rev. Sci. Instrum. 66, 48-51
27. Morgan, C. G., Hua, Y., Mitchell, A. C., Murray, J. G., and Boardman, A. D. (1996) Rev. Sci. Instrum. 67, 41-47
28. Gryczynski, I., Malak, H., and Lakowicz, J. R. (1996) Biospectroscopy 2, 9-15
29. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, pp. 5.68-5.72, Cold Spring Harbor, New York
30. Carra, J. H., and Privalov, P. L. (1997) Biochemistry 36, 526-535
31. Damante, G., Tell, G., Leonardi, A., Fogolari, F., Bortolotti, N., Di Lauro, R., and Formisano, S. (1994) FEBS Lett. 354, 293-296
32. Chakrabartty, A., Kortemme, T., Padmanabhan, S., and Baldwin, R. L. (1993) Biochemistry 32, 5560-5565
33. Woody, R. W. (1978) Biopolymers 17, 1451-1467
34. Otting, G., Qian, Y. Q., Muller, M., Affolter, M., Gehring, W., and Wuthrich, K. (1988) EMBO J. 7, 4305-4309
35. Peitsch, M. C. (1995) Bio-Technology 13, 658-660
36. Peitsch, M. C. (1996) Biochem. Soc. Trans. 24, 274-279
37. Fraenkel, E., Rould, M. A., Chambers, K. A., and Pabo, C. O. (1998) J. Mol. Biol. 284, 351-361
38. Fernando, T., and Royer, C. A. (1992) Biochemistry 31
39. Rouviere, N., Vincent, M., Craesu, C. T., and Gallay, J. (1997) Biochemistry 36, 7339-7352
40. Levitt, M., and Perutz, M. F. (1988) J. Mol. Biol. 201, 751-754
41. Burley, S. K., and Petsko, G. (1986) FEBS Lett. 203, 139-143
42. Suwaiyan, A., and Klein, U. K. A. (1989) Chem. Phys. Lett. 159, 244-250
43. Van Duuren, B. L. (1961) J. Org. Chem. 26, 2954-2960
44. Laughon, A. (1991) Biochemistry 30, 11357-11367
45. Chen, Y., and Barkley, M. D. (1998) Biochemistry 37, 9976-9982