Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions
(2019) In Science Advances 5(7).- Abstract
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... (More)
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.
(Less)
- author
- organization
- publishing date
- 2019-07-17
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Science Advances
- volume
- 5
- issue
- 7
- article number
- eaaw1531
- publisher
- American Association for the Advancement of Science (AAAS)
- external identifiers
-
- scopus:85069837025
- pmid:31328161
- ISSN
- 2375-2548
- DOI
- 10.1126/sciadv.aaw1531
- language
- English
- LU publication?
- yes
- id
- 57ceace5-761d-4710-8f29-681f2341f5e4
- date added to LUP
- 2019-08-29 15:10:59
- date last changed
- 2024-10-02 11:17:37
@article{57ceace5-761d-4710-8f29-681f2341f5e4, abstract = {{<p>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.</p>}}, author = {{Berntsson, Oskar and Rodriguez, Ryan and Henry, Léocadie and Panman, Matthijs R. and Hughes, Ashley J. and Einholz, Christopher and Weber, Stefan and Ihalainen, Janne A. and Henning, Robert and Kosheleva, Irina and Schleicher, Erik and Westenhoff, Sebastian}}, issn = {{2375-2548}}, language = {{eng}}, month = {{07}}, number = {{7}}, publisher = {{American Association for the Advancement of Science (AAAS)}}, series = {{Science Advances}}, title = {{Photoactivation of Drosophila melanogaster cryptochrome through sequential conformational transitions}}, url = {{http://dx.doi.org/10.1126/sciadv.aaw1531}}, doi = {{10.1126/sciadv.aaw1531}}, volume = {{5}}, year = {{2019}}, }