Structural insights into the activity of enhancer-binding proteins

Science

Volumn 307, Issue 5717, 2005, Pages 1972-1975

  Rappas, Mathieu ^a   Schumacher, Jorg ^a   Beuron, Fabienne ^a   Niwa, Hajime ^a   Bordes, Patricia ^a   Wigneshweraraj, Sivaramesh ^a   Keetch, Catherine A ^b   Robinson, Carol V ^b   Buck, Martin ^a   Zhang, Xiaodong ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; BACTERIA; CONFORMATIONS; CRYOGENICS; CRYSTAL STRUCTURE; ELECTRON MICROSCOPY; ENZYMES; HYDROLYSIS; RNA;

ADENOSINE TRIPHOSPHATE (ATP) HYDROLYSIS; BASAL FACTORS; CRYOGENIC ELECTRON MICROSCOPY (CRYO-EM); ENHANCER-BINDING PROTEINS;

PROTEINS;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BACTERIAL DNA; BACTERIAL PROTEIN; BINDING PROTEIN; ENHANCER BINDING PROTEIN; HOLOENZYME; PROTEIN PSPF; RNA POLYMERASE; SIGMA FACTOR; UNCLASSIFIED DRUG;

BIOLOGY;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; ELECTROSPRAY MASS SPECTROMETRY; ENHANCER REGION; ESCHERICHIA COLI; GENE EXPRESSION REGULATION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN STRUCTURE; TRANSCRIPTION REGULATION;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CRYOELECTRON MICROSCOPY; CRYSTALLOGRAPHY, X-RAY; DNA-BINDING PROTEINS; DNA-DIRECTED RNA POLYMERASES; ESCHERICHIA COLI PROTEINS; HYDROLYSIS; HYDROPHOBICITY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PII NITROGEN REGULATORY PROTEINS; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RNA POLYMERASE SIGMA 54; SIGMA FACTOR; TRANS-ACTIVATORS; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 20144366027     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1105932     Document Type: Article

References (30)

1. I. Rombel, A. North, I. Hwang, C. Wyman, S. Kustu, Cold Spring Harbor Symp. Quant. Biol. 63, 1S7 (1998).
2. M. Buck, M. T. Gallegos, D. J. Studholme, Y. Guo, J. D. Gralla, J. Bacteriol. 182, 4129 (2000).
3. X. Zhang et al., Mol. Microbiol. 45, 89S (2002).
4. A. Wedel, S. Kustu, Genes Dev. 9, 2042 (1995).
5. D. L. Popham, D. Szeto, J. Keener, S. Kustu, Science 243, 629 (1989).
6. W. V. Cannon, M. T. Gallegos, M. Buck, Nat. Struct. Biol. 7, 594 (2000).
7. H. Xu, T. R. Hoover, Curr. Opin. Microbiol. 4, 138 (2001).
8. E. Morett, L. Segovia, J. Bacteriol. 175, 6067 (1993).
9. D. J. Studholme, R. Dixon, J. Bacteriol. 185, 1757 (2003).
10. A. N. Lupas, J. Martin, Curr. Opin. Struct. Biol. 12, 746 (2002).
11. A. F. Neuwald, L. Aravind, J. L. Spouge, E. V. Koonin, Genome Res. 9, 27 (1939).
12. T. Ogura, A. J. Wilkinson, Genes Cells 6, 575 (2001).
13. S. Y. Lee et al., Genes Dev. 17, 2552 (2003).
14. M. Chaney et al., Genes Dev. 15, 2282 (2001).
15. W. Cannon, P. Bordes, S. R. Wigneshweraraj, M. Buck, J. Biol. Chem. 278, 19815 (2003).
16. Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; K, Lys; L, Leu; Q, Gln; R, Arg; S, Ser; T, Thr; V, Val; and W, Trp.
17. Y. K. Wang, J. H. Lee, J. M. Brewer, T. R. Hoover, Mol. Microbiol. 26, 373 (1997).
18. P. Bordes et al., Proc. Natl. Acad. Sci. U.S.A. 100, 2278 (2003).
19. V. Gonzalez, L. Olvera, X. Soberon, E. Morett, Mol. Microbiol. 28, 55 (1998).
20. F. Beuron et al., J. Mol. Biol. 327, 619 (2003).
21. J. Furst, R. B. Sutton, J. Chen, A. T. Brunger, N. Grigorieff, EMBO J. 22, 4365 (2003).
22. D. I. Svergun, M. Malfois, M. H. Koch, S. R. Wigneshweraraj, M. Buck, J. Biol. Chem. 275, 4210 (2000).
23. K. S. Murakami, S. Masuda, S. A. Darst, Science 296, 1280 (2002).
24. P. C. Burrows, K. Severinov, A. Ishihama, M. Buck, S. R. Wigneshweraraj, J. Biol. Chem. 278, 29728 (2003).
25. Materials and methods are available as supporting material on Science Online.
26. J. Wang et al., Structure (Cambridge) 9, 1107 (2001).
27. P. Bordes, S. R. Wigneshweraraj, X. Zhang, M. Buck, Biochem. J. 378, 735 (2004).
28. Y. K. Wang, T. R. Hoover, J. Bacteriol. 179, 5812 (1997).
29. J. Li, L. Passaglia, I. Rombel, D. Yan, S. Kustu, J. Bacteriol. 181, 5443 (1999).
30. We thank the members of M.B. and X.Z.'s laboratories for their help and useful discussions throughout this work; I. Leiros at The European Synchrotron Radiation Facility and beamline scientists at Daresbury for their help in data collection; and Imperial College Centre for Biomolecular Electron Microscopy for support. This work is supported by Biotechnology and Biological Sciences Research Council funding to X.Z. and M.B. Coordinates for the reported structures have been deposited in the Protein Data Bank with accession codes 2BJW and 2BJV. The EM map has been deposited in the electron microscopy database (EMDB) with accession code EMD-1109.