Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

The cryptochromes.

Chentao Lin1, Takeshi Todo

  • 1Department of Molecular, Cell and Developmental Biology, University of California, Los Angeles, 621 Charles Young Drive South, Los Angeles, CA 90095-1606, USA. clin@mcdb.ucla.edu

Genome Biology
|May 17, 2005
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A CRY1 Interactor eIF3G1 Negatively Regulates Root Growth Under Blue Light in <i>Arabidopsis</i>.

Plants (Basel, Switzerland)·2026
Same author

A cost-effective dual reporter system in <i>Nicotiana benthamiana</i>.

Frontiers in plant science·2026
Same author

Brain-derived estrogens facilitate male-typical behaviors by potentiating androgen receptor signaling in medaka.

eLife·2026
Same author

6-4 photolyase differentially modulates transcription in the vertebrate circadian clock.

PLoS genetics·2025
Same author

<i>De Novo</i> Biosynthesis of Neoxanthin in Engineered <i>Escherichia coli</i>.

ACS synthetic biology·2025
Same author

Immunogenicity and protective efficacy of Vibrio vulnificus outer membrane vesicles in zebrafish: Implications for fish immunization.

Fish & shellfish immunology·2025
Same journal

UK Biobank whole-genome sequencing reveals robust contributions of rare variants to complex-trait heritability.

Genome biology·2026
Same journal

A one-week automated genome-wide optical pooled screen using OttoSeq.

Genome biology·2026
Same journal

Integrated lipidomic and transcriptomic profiling of the host response in human malaria.

Genome biology·2026
Same journal

Centromeric satellite expansion drives genome evolution in the snowy owl.

Genome biology·2026
Same journal

Mapping the landscape of allele-specific expression in porcine genomes.

Genome biology·2026
Same journal

Genomic sequence evolution underlying human neocortical interareal diversification.

Genome biology·2026
See all related articles

Cryptochromes are light-sensing proteins crucial for circadian rhythms in plants and animals. Their structure, similar to DNA repair enzymes, suggests an evolutionary link and a shared functional mechanism involving flavin adenine dinucleotide (FAD).

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Chronobiology

Background:

  • Cryptochromes are essential photoreceptors regulating circadian clocks in diverse organisms.
  • They play roles in plant photomorphogenesis and are integral to animal circadian oscillators.
  • Cryptochromes are evolutionarily linked to DNA photolyases, light-activated DNA repair enzymes.

Purpose of the Study:

  • To elucidate the structural and functional relationship between cryptochromes and DNA photolyases.
  • To understand the role of the flavin adenine dinucleotide (FAD) chromophore and its binding site in cryptochrome function.
  • To explore the evolutionary origins of cryptochromes from DNA repair enzymes.

Main Methods:

  • Comparative structural analysis of cryptochromes and photolyases.

Related Experiment Videos

  • Bioinformatic approaches to identify conserved domains and motifs.
  • Biochemical studies to investigate chromophore binding and catalytic mechanisms (predicted).

    • Main Results:

    • Cryptochromes and photolyases share conserved structural features, including alpha/beta and helical domains.
    • Both protein families bind the flavin adenine dinucleotide (FAD) chromophore.
    • The FAD-access cavity in the helical domain is identified as a potentially crucial functional site for both enzyme types.

    Conclusions:

    • Cryptochromes likely evolved from DNA photolyases, inheriting a core structural and functional framework.
    • The FAD-binding site is central to the mechanism of action for both cryptochromes and photolyases.
    • Understanding these structural similarities provides insights into the evolution of light-sensing and DNA repair mechanisms.