Journal
SCIENCE ADVANCES
Volume 5, Issue 7, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.aaw1531
Keywords
-
Categories
Funding
- Swedish Foundation for International Cooperation in Research and Higher Education
- European Research Council [725642]
- Foundation of Strategic Research, Sweden
- DFG [235777276/GRK1976]
- Academy of Finland [296135]
- Jane and Aatos Erkko Foundation
- Academy of Finland (AKA) [296135, 296135] Funding Source: Academy of Finland (AKA)
- European Research Council (ERC) [725642] Funding Source: European Research Council (ERC)
Ask authors/readers for more resources
Cryptochromes are blue-light photoreceptor proteins, which provide input to circadian clocks. The cryptochrome from Drosophila melanogaster (DmCry) modulates the degradation of Timeless and itself. It is unclear how light absorption by the chromophore and the subsequent redox reactions trigger these events. Here, we use nano- to millisecond time-resolved x-ray solution scattering to reveal the light-activated conformational changes in DmCry and the related (6-4) photolyase. DmCry undergoes a series of structural changes, culminating in the release of the carboxyl-terminal tail (CTT). The photolyase has a simpler structural response. We find that the CTT release in DmCry depends on pH. Mutation of a conserved histidine, important for the biochemical activity of DmCry, does not affect transduction of the structural signal to the CTT. Instead, molecular dynamics simulations suggest that it stabilizes the CTT in the resting-state conformation. Our structural photocycle unravels the first molecular events of signal transduction in an animal cryptochrome.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available