Evidence map›Paper›PMID 21875594›Full record

ArticleJournal of molecular biology2011

Light-induced conformational changes in full-length Arabidopsis thaliana cryptochrome.

Masato Kondoh, Chiaki Shiraishi, Pavel Müller, Margaret Ahmad, Kenichi Hitomi, Elizabeth D Getzoff, Masahide Terazima

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
8.2field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  5. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  6. Review
  7. Dimerization of European Robin Cryptochrome 4a.The journal of physical chemistry. B · 2023
    Article
  8. Article
  9. Article
  10. Activation mechanism ofScience advances · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Structural disorder in plant proteins: where plasticity meets sessility.Cellular and molecular life sciences : CMLS · 2017
    Review
  17. Hyperactivity of theThe Journal of biological chemistry · 2017
    Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Masato KondohDepartment of Chemistry, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan.
Chiaki Shiraishi
Pavel Müller
Margaret Ahmad
Kenichi Hitomi
Elizabeth D Getzoff
Masahide Terazima
Kyoto University · JPScripps Research Institute · USSorbonne Université · FR

Funding

STRUCTURAL ANALYSIS OF CHROMATICALLY ACTIVE PROTEINSR01GM037684 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GETZOFF, ELIZABETH D · 1987 to 2009
$3.1M
NIGMS NIH HHS GM37684NIGMS NIH HHS R01 GM037684
6 · The paper itself

Abstract

Cryptochromes (CRYs) are widespread flavoproteins with homology to photolyases (PHRs), a class of blue-light-activated DNA repair enzymes. Unlike PHRs, both plant and animal CRYs have a C-terminal domain. This cryptochrome C-terminal (CCT) domain mediates interactions with other proteins, while the PHR-like domain converts light energy into a signal via reduction and radical formation of the flavin adenine dinucleotide cofactor. However, the mechanism by which the PHR-like domain regulates the CCT domain is not known. Here, we applied the pulsed-laser-induced transient grating method to detect conformational changes induced by blue-light excitation of full-length Arabidopsis thaliana cryptochrome 1 (AtCRY1). A significant reduction in the diffusion coefficient of AtCRY1 was observed upon photoexcitation, indicating that a large conformational change occurs in this monomeric protein. AtCRY1 containing a single mutation (W324F) that abolishes an intra-protein electron transfer cascade did not exhibit this conformational change. Moreover, the conformational change was much reduced in protein lacking the CCT domain. Thus, we conclude that the observed large conformational changes triggered by light excitation of the PHR-like domain result from C-terminal domain rearrangement. This inter-domain modulation would be critical for CRYs' ability to transduce a blue-light signal into altered protein-protein interactions for biological activity. Lastly, we demonstrate that the transient grating technique provides a powerful method for the direct observation and understanding of photoreceptor dynamics.

Indexed as

LightAmino Acid SubstitutionArabidopsisArabidopsis ProteinsCryptochromesModels, BiologicalModels, ChemicalMutant ProteinsProtein ConformationArabidopsis ProteinsCRY1 protein, ArabidopsisCryptochromesMutant Proteins

Identifiers

PMID21875594
PMCPMC4451184
OpenAlexW2029717929

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.