Single chain forms of the enhancer binding protein pspf provide insights into geometric requirements for gene activation

Journal of Biological Chemistry

Volumn 286, Issue 14, 2011, Pages 12734-12742

  Joly, Nicolas ^a   Buck, Martin ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTIVE RESPONSE; BACTERIAL PATHOGENESIS; DIFFERENTIAL CONTRIBUTION; DNA MELTING; ENHANCER BINDING PROTEINS; GENE ACTIVATION; GENETIC INFORMATION; HEXAMERIC ATPASE; HEXAMERS; MODE OF ACTION; RNA POLYMERASE; SINGLE CHAINS; SINGLE-STRANDED DNA;

BACTERIOLOGY; CHEMICAL ACTIVATION; COORDINATION REACTIONS; DNA; GENES; NUCLEIC ACIDS; OLIGOMERS; PROTEINS; RNA;

TRANSCRIPTION;

ADENOSINE TRIPHOSPHATASE; BACTERIAL PROTEIN; ENHANCER BINDING PROTEIN PSPF; OLIGOMER; POLYPEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; GENE ACTIVATION; GEOMETRY; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TARGETING;

ADENOSINE TRIPHOSPHATASES; CHROMATOGRAPHY, GEL; DNA-DIRECTED RNA POLYMERASES; ESCHERICHIA COLI PROTEINS; MODELS, THEORETICAL; TRANS-ACTIVATORS; TRANSCRIPTIONAL ACTIVATION;

BACTERIA (MICROORGANISMS);

EID: 79953326554     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.203554     Document Type: Article

References (41)

1. Tucker, P. A., and Sallai, L. (2007) Curr. Opin. Struct. Biol. 17, 641-652
2. Erzberger, J. P., and Berger, J. M. (2006) Annu Rev Biophys Biomol Struct. 35, 93-114
3. Ogura, T., and Wilkinson, A. J. (2001) Genes Cells. 6, 575-597
4. Iyer, L. M., Leipe, D. D., Koonin, E. V., and Aravind, L. (2004) Journal of structural biology. 146, 11-31
5. Ogura, T., Matsushita-Ishiodori, Y., Johjima, A., Nishizono, M., Nishikori, S., Esaki, M., and Yamanaka, K. (2008) Biochem. Soc. Trans. 36, 68-71
6. Schumacher, J., Joly, N., Rappas, M., Zhang, X., and Buck, M. (2006) J. Struct. Biol. 156, 190-199
7. Neuwald, A. F., Aravind, L., Spouge, J. L., and Koonin, E. V. (1999) Genome Res. 9, 27-43
8. Bell, S. P., and Dutta, A. (2002) Annu. Rev. Biochem. 71, 333-374
9. Forsburg, S. L. (2004) Microbiol Mol. Biol. Rev. 68, 109-131
10. Bochman, M. L., and Schwacha, A. (2008) Mol. Cell 31, 287-293
11. Schwacha, A., and Bell, S. P. (2001) Mol. Cell 8, 1093-1104
12. Barry, E. R., Lovett, J. E., Costa, A., Lea, S. M., and Bell, S. D. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 1051-1056
13. Joly, N., and Buck, M. (2010) J. Biol. Chem. 285, 15178-15186
14. Moreau, M. J., McGeoch, A. T., Lowe, A. R., Itzhaki, L. S., and Bell, S. D. (2007) Mol. Cell 28, 304-314
15. Martin, A., Baker, T. A., and Sauer, R. T. (2008) Nat. Struct. Mol. Biol. 15, 139-145
16. Martin, A., Baker, T. A., and Sauer, R. T. (2005) Nature 437, 1115-1120
17. Model, P., Jovanovic, G., and Dworkin, J. (1997) Mol. Microbiol. 24, 255-261
18. Jovanovic, G., and Model, P. (1997) Mol. Microbiol. 25, 473-481
19. Wigneshweraraj, S. R., Burrows, P. C., Bordes, P., Schumacher, J., Rappas, M., Finn, R. D., Cannon, W. V., Zhang, X., and Buck, M. (2005) Prog. Nucleic. Acids. Res. Mol. Biol. 79, 339-369
20. Buck, M., and Cannon, W. (1992) Nature 358, 422-424
21. Buck, M., Gallegos, M. T., Studholme, D. J., Guo, Y., and Gralla, J. D. (2000) J. Bacteriol. 182, 4129-4136
22. Merrick, M. J. (1993) Mol. Microbiol. 10, 903-909
23. Zhang, X., Chaney, M., Wigneshweraraj, S. R., Schumacher, J., Bordes, P., Cannon, W., and Buck, M. (2002) Mol. Microbiol. 45, 895-903
24. Ishihama, A. (2000) Ann. Rev. Microbiol. 54, 499-518
25. Bose, D., Pape, T., Burrows, P. C., Rappas, M., Wigneshweraraj, S. R., Buck, M., and Zhang, X. (2008) Mol. Cell 32, 337-346
26. Chaney, M., Grande, R., Wigneshweraraj, S. R., Cannon, W., Casaz, P., Gallegos, M. T., Schumacher, J., Jones, S., Elderkin, S., Dago, A. E., Morett, E., and Buck, M. (2001) Genes Dev. 15, 2282-2294
27. Rappas, M., Schumacher, J., Beuron, F., Niwa, H., Bordes, P., Wigneshweraraj, S., Keetch, C. A., Robinson, C. V., Buck, M., and Zhang, X. (2005) Science 307, 1972-1975
28. Burrows, P. C., Joly, N., and Buck, M. (2010) Proc. Natl. Acad. Sci. U.S.A. 107, 9376-9381
29. Joly, N., Schumacher, J., and Buck, M. (2006) J. Biol. Chem. 281, 34997-35007
30. Bordes, P., Wigneshweraraj, S. R., Schumacher, J., Zhang, X., Chaney, M., and Buck, M. (2003) Proc. Natl. Acad. Sci. U.S.A. 100, 2278-2283
31. Martin, A., Baker, T. A., and Sauer, R. T. (2008) Nat. Struct. Mol. Biol. 15, 1147-1151
32. Martin, A., Baker, T. A., and Sauer, R. T. (2008) Mol. Cell 29, 441-450
33. Rappas, M., Schumacher, J., Niwa, H., Buck, M., and Zhang, X. (2006) J. Mol. Biol. 357, 481-492
34. Hoskins, J. R., Doyle, S. M., and Wickner, S. (2009) Proc. Natl. Acad. Sci. U.S.A. 106, 22233-22238
35. Thomsen, N. D., and Berger, J. M. (2009) Cell 139, 523-534
36. Glynn, S. E., Martin, A., Nager, A. R., Baker, T. A., and Sauer, R. T. (2009) Cell 139, 744-756
37. Hersch, G. L., Burton, R. E., Bolon, D. N., Baker, T. A., and Sauer, R. T. (2005) Cell 121, 1017-1027
38. Roberts, A. J., Numata, N., Walker, M. L., Kato, Y. S., Malkova, B., Kon, T., Ohkura, R., Arisaka, F., Knight, P. J., Sutoh, K., and Burgess, S. A. (2009) Cell 136, 485-495
39. Mott, M. L., Erzberger, J. P., Coons, M. M., and Berger, J. M. (2008) Cell 135, 623-634
40. Cannon, W. V., Gallegos, M. T., and Buck, M. (2000) Nat. Struct. Biol. 7, 594-601
41. Nørby, J. G. (1988) Methods Enzymol. 156, 116-119