Single amino acid substitution reveals latent photolyase activity in arabidopsis cry1

Angewandte Chemie - International Edition

Volumn 51, Issue 37, 2012, Pages 9356-9360

  Burney, Sarah ^a   Wenzel, Ringo ^b   Kottke, Tilman ^c   Roussel, Thomas ^a   Hoang, Nathalie ^a   Bouly, Jean Pierre ^a   Bittl, Robert ^b   Heberle, Joachim ^b   Ahmad, Margaret ^a  

^a SORBONNE UNIVERSITÉ   (France)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

^c BIELEFELD UNIVERSITY   (Germany)

Author keywords

biophysics; cryptochromes; DNA damage; flavin reduction; photochemistry

Indexed keywords

AMINO ACID SUBSTITUTION; ARABIDOPSIS; CONSERVED RESIDUES; CRYPTOCHROMES; DNA DAMAGES; IN-VITRO; MUTANT PROTEINS; PHOTO-REDUCTION; PHOTOLYASES; SINGLE-STRANDED DNA; WILD TYPES;

BIOPHYSICS; DNA; PHOTOCHEMICAL REACTIONS;

AMINO ACIDS;

ARABIDOPSIS PROTEIN; CRY1 PROTEIN, ARABIDOPSIS; CRYPTOCHROME; RIBOFLAVIN DERIVATIVE;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ARTICLE; CHEMISTRY; DNA REPAIR; ENZYMOLOGY; GENETICS; METABOLISM; OXIDATION REDUCTION REACTION; ULTRAVIOLET RADIATION;

AMINO ACID SUBSTITUTION; ARABIDOPSIS; ARABIDOPSIS PROTEINS; CRYPTOCHROMES; DNA REPAIR; FLAVINS; OXIDATION-REDUCTION; ULTRAVIOLET RAYS;

EID: 84865840972     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201203476     Document Type: Article

References (22)

1. A. Sancar, Chem. Rev. 2003, 103, 2203-2237.
2. C. Lin, T. Todo, Genome Biol. 2005, 6, 220.
3. I. Chaves, R. Pokorny, M. Byrdin, N. Hoang, T. Ritz, K. Brettel, L. O. Essen, G. T. van der Horst, A. Batschauer, M. Ahmad, Annu. Rev. Plant Biol. 2011, 62, 335-364.
4. N. Ozturk, J. H. Lee, S. Gaddameedhi, A. Sancar, Proc. Natl. Acad. Sci. USA 2009, 106, 2841-2846.
5. A. E. Hoffman, T. Zheng, C. H. Yi, R. G. Stevens, Y. Ba, Y. Zhang, D. Leaderer, T. Holford, J. Hansen, Y. Zhu, Cancer Prev. Res. 2010, 3, 539-548.
6. M. Müller, T. Carell, Curr. Opin. Struct. Biol. 2009, 19, 277-285.
7. L. O. Essen, Curr. Opin. Struct. Biol. 2006, 16, 51-59.
8. J. P. Bouly, E. Schleicher, M. Dionisio-Sese, F. Vandenbussche, D. Van Der Straeten, N. Bakrim, S. Meier, A. Batschauer, P. Galland, R. Bittl, M. Ahmad, J. Biol. Chem. 2007, 282, 9383-9391.
9. R. Banerjee, E. Schleicher, S. Meier, R. M. Viana, R. Pokorny, M. Ahmad, R. Bittl, A. Batschauer, J. Biol. Chem. 2007, 282, 14916-14922.
10. A. Berndt, T. Kottke, H. Breitkreuz, R. Dvorsky, S. Hennig, M. Alexander, E. Wolf, J. Biol. Chem. 2007, 282, 13011-13021.
11. N. Hoang, E. Schleicher, S. Kacprzak, J. P. Bouly, M. Picot, W. Wu, A. Berndt, E. Wolf, R. Bittl, M. Ahmad, PLoS Biol. 2008, 6, e 160.
12. X. Li, Q. Wang, X. Yu, H. Liu, H. Yang, C. Zhao, X. Liu, C. Tan, J. Klejnot, D. Zhong, C. Lin, Proc. Natl. Acad. Sci. USA 2011, 108, 20844-20849.
13. E. N. Worthington, I. H. Kavakli, G. Benocal-Tito, A. Sancar, J. Biol. Chem. 2003, 278, 39143-39154.
14. V. Balland, M. Byrdin, A. P. Eker, M. Ahmad, K. Brettel, J. Am. Chem. Soc. 2009, 131, 426-427.
15. T. Kottke, A. Batschauer, M. Ahmad, J. Heberle, Biochemistry 2006, 45, 2472-2479.
16. C. P. Selby, A. Sancar, Proc. Natl. Acad. Sci. USA 2006, 103, 17696-17700.
17. N. Ozturk, C. P. Selby, Y. Annayev, D. Zhong, A. Sancar, Proc. Natl. Acad. Sci. USA 2011, 108, 516-521.
18. L. Xu, W. Mu, Y. Ding, Z. Luo, Q. Han, F. Bi, Y. Wang, Q. Song, Biochemistry 2008, 47, 8736-8743.
19. H. Q. Yang, Y. J. Wu, R. H. Tang, D. Liu, Y. Liu, A. R. Cashmore, Cell 2000, 103, 815-827.
20. H. Liu, X. Yu, K. Li, J. Klejnot, H. Yang, D. Lisiero, C. Lin, Science 2008, 322, 1535-1539.
21. E. Rosato, V. Codd, G. Mazzotta, A. Piccin, M. Zordan, R. Costa, C. P. Kyriacou, Curr. Biol. 2001, 11, 909-917.
22. M. Kondoh, C. Shiraishi, P. Müller, M. Ahmad, K. Hitomi, E. D. Getzoff, M. Terazima, J. Mol. Biol. 2011, 413, 128-137.