Allosteric transcriptional regulation via changes in the overall topology of the core promoter

Science

Volumn 349, Issue 6250, 2015, Pages 877-881

  Philips, Steven J ^a   Canalizo Hernandez, Monica ^a   Yildirim, Ilyas ^a   Schatz, George C ^a   Mondragón, Alfonso ^a   O'Halloran, Thomas V ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ESCHERICHIA COLI PROTEIN; MERR PROTEIN; REGULATOR PROTEIN; REGULATORY PROTEIN CUER; RNA POLYMERASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DNA BINDING PROTEIN; DNA DIRECTED RNA POLYMERASE; MERR PROTEIN, BACTERIA;

ION; NUCLEIC ACID; POLYMERASE CHAIN REACTION; PROKARYOTE; PROTEIN; SUBSTRATE; TOPOLOGY;

ALLOSTERISM; ARTICLE; BINDING SITE; CRYSTALLIZATION; DNA CONFORMATION; DNA STRUCTURE; ENZYME SUBSTRATE; ESCHERICHIA COLI; MECHANICAL TORSION; METAL BINDING; MOLECULAR DYNAMICS; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN CONFORMATION; PROTEIN DNA BINDING; REPRESSOR GENE; STEREOCHEMISTRY; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION; CHEMISTRY; CONFORMATION; GENETIC TRANSCRIPTION; GENETICS; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

PROKARYOTA;

ALLOSTERIC REGULATION; ALLOSTERIC SITE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DNA; DNA-BINDING PROTEINS; DNA-DIRECTED RNA POLYMERASES; NUCLEIC ACID CONFORMATION; PROMOTER REGIONS, GENETIC; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; TRANSCRIPTION, GENETIC; TRANSCRIPTIONAL ACTIVATION;

EID: 84939832273     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaa9809     Document Type: Article

References (27)

1. R. Rohs et al., Annu. Rev. Biochem. 79, 233-269 (2010).
2. R. Schleif, FEMS Microbiol. Rev. 34, 779-796 (2010).
3. N. L. Brown, J. V. Stoyanov, S. P. Kidd, J. L. Hobman, FEMS Microbiol. Rev. 27, 145-163 (2003).
4. Z. Ma, F. E. Jacobsen, D. P. Giedroc, Chem. Rev. 109, 4644-4681 (2009).
5. A. Z. Ansari, J. E. Bradner, T. V. O'Halloran, Nature 374, 370-375 (1995).
6. C. E. Outten, F. W. Outten, T. V. O'Halloran, J. Biol. Chem. 274, 37517-37524 (1999).
7. B. Frantz, T. V. O'Halloran, Biochemistry 29, 4747-4751 (1990).
8. E. E. Heldwein, R. G. Brennan, Nature 409, 378-382 (2001).
9. K. J. Newberry, R. G. Brennan, J. Biol. Chem. 279, 20356-20362 (2004).
10. S. Watanabe, A. Kita, K. Kobayashi, K. Miki, Proc. Natl. Acad. Sci. U.S.A. 105, 4121-4126 (2008).
11. F. W. Outten, C. E. Outten, J. Hale, T. V. O'Halloran, J. Biol. Chem. 275, 31024-31029 (2000).
12. A. Changela et al., Science 301, 1383-1387 (2003).
13. J. V. Stoyanov, J. L. Hobman, N. L. Brown, Mol. Microbiol. 39, 502-512 (2001).
14. C. Petersen, L. B. Møller, Gene 261, 289-298 (2000).
15. K. Yamamoto, A. Ishihama, Mol. Microbiol. 56, 215-227 (2005).
16. G. Guzikevich-Guerstein, Z. Shakked, Nat. Struct. Biol. 3, 32-37 (1996).
17. W. Ross, S. J. Park, A. O. Summers, J. Bacteriol. 171, 4009-4018 (1989).
18. K. M. Comess, L. M. Shewchuk, K. Ivanetich, C. T. Walsh, Biochemistry 33, 4175-4186 (1994).
19. J. Parkhill, A. Z. Ansari, J. G. Wright, N. L. Brown, T. V. O'Halloran, EMBO J. 12, 413-421 (1993).
20. N. M. Andoy et al., Biophys. J. 97, 844-852 (2009).
21. T. V. O'Halloran, B. Frantz, M. K. Shin, D. M. Ralston, J. G. Wright, Cell 56, 119-129 (1989).
22. A. O. Summers, Curr. Opin. Microbiol. 12, 138-144 (2009).
23. C. Liu, E. Kim, B. Demple, N. C. Seeman, Biochemistry 51, 937-943 (2012).
24. A. Z. Ansari, M. L. Chael, T. V. O'Halloran, Nature 355, 87-89 (1992).
25. K. S. Murakami, S. Masuda, E. A. Campbell, O. Muzzin, S. A. Darst, Science 296, 1285-1290 (2002).
26. Y. Zhang et al., Science 338, 1076-1080 (2012).
27. A. Feklistov, S. A. Darst, Cell 147, 1257-1269 (2011).