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Related Concept Videos

Exon Recombination02:32

Exon Recombination

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The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
Exon shuffling follows “splice frame rules.” Each exon...
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Related Experiment Video

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Circadian Entrainment of Drosophila Melanogaster
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Flavin reduction activates Drosophila cryptochrome.

Anand T Vaidya1, Deniz Top, Craig C Manahan

  • 1Department of Chemistry and Chemical Biology and Biotechnology Resource Center, Cornell University, Ithaca, NY 14853.

Proceedings of the National Academy of Sciences of the United States of America
|December 4, 2013
PubMed
Summary
This summary is machine-generated.

Light triggers conformational changes in Drosophila cryptochrome (dCRY) by reducing its flavin cofactor, impacting circadian rhythms. This photoreduction releases the C-terminal tail, facilitating interactions with the Timeless protein and potentially activating CRY signaling.

Keywords:
photolyaseprotein-protein interactionredox

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Area of Science:

  • Chronobiology
  • Molecular Biology
  • Photochemistry

Background:

  • Circadian rhythms in higher organisms are regulated by light-sensing proteins and cellular oscillators.
  • Drosophila cryptochrome (dCRY) is a key photoreceptor in the fly circadian clock, featuring a critical C-terminal tail (CTT) involved in light signaling.

Purpose of the Study:

  • To elucidate the molecular mechanism by which light activates Drosophila cryptochrome (dCRY).
  • To investigate the role of the C-terminal tail (CTT) and flavin cofactor in dCRY's light response and interaction with Timeless (TIM).

Main Methods:

  • Utilized proteolytic susceptibility assays and small-angle X-ray scattering (SAXS) to study dCRY conformational changes.
  • Investigated the effects of light and chemical reduction on dCRY structure and function.
  • Examined the interaction between dCRY and the Timeless (TIM) protein.

Main Results:

  • Light-induced reduction of the dCRY flavin cofactor to an anionic semiquinone (ASQ) radical alters protein conformation, affecting the CTT.
  • This conformational change increases CTT proteolytic susceptibility and is mimicked by chemical reduction.
  • Photoreduction releases the dCRY CTT, promoting binding to Timeless (TIM) and suggesting a general CRY activation mechanism via flavin reduction.

Conclusions:

  • Flavin reduction, triggered by light or cellular reductants, is a key mechanism for CRY activation.
  • The conformational response of dCRY upon flavin reduction involves both the CTT and remote regions.
  • dCRY's light signaling pathway is intricately linked to its redox state and interactions with partner proteins like TIM.