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Structure of full-length Drosophila cryptochrome

Author

Listed:
  • Brian D. Zoltowski

    (Cornell University)

  • Anand T. Vaidya

    (Cornell University)

  • Deniz Top

    (Laboratory of Genetics, The Rockefeller University)

  • Joanne Widom

    (Cornell University)

  • Michael W. Young

    (Laboratory of Genetics, The Rockefeller University)

  • Brian R. Crane

    (Cornell University)

Abstract

Structure of a circadian photoreceptor The cryptochrome/photolyase family of photoreceptors mediates cellular responses to ultraviolet and blue light exposure in all kingdoms of life: cryptochromes transduce signals important for growth, development, magnetosensitivity and circadian clocks, and photolyases repair photolesions in DNA. Zoltowski et al. have now solved the X-ray crystal structure of full-length cryptochrome from Drosophila. They find that a C-terminal helix docks in a groove that is known to bind DNA substrates in photolyases, and a conserved tryptophan protrudes into the catalytic centre of the cryptochrome, mimicking how DNA-repair photolyases recognize lesions in DNA.

Suggested Citation

  • Brian D. Zoltowski & Anand T. Vaidya & Deniz Top & Joanne Widom & Michael W. Young & Brian R. Crane, 2011. "Structure of full-length Drosophila cryptochrome," Nature, Nature, vol. 480(7377), pages 396-399, December.
    • Handle: RePEc:nat:nature:v:480:y:2011:i:7377:d:10.1038_nature10618
    DOI: 10.1038/nature10618
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    Cited by:

    1. Zhiwei Zhao & Craig Dent & Huafeng Liang & Junqing Lv & Guandong Shang & Yawen Liu & Fan Feng & Fei Wang & Junhong Pang & Xu Li & Libang Ma & Bing Li & Sridevi Sureshkumar & Jia-Wei Wang & Sureshkumar, 2022. "CRY2 interacts with CIS1 to regulate thermosensory flowering via FLM alternative splicing," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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