Evidence map›Paper›PMID 24475227›Full record

ArticlePloS one2014

Factors that control the chemistry of the LOV domain photocycle.

Josiah P Zayner, Tobin R Sosnick

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
12.1field-weighted citation impact, top 2% 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

64 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Hydraulic Activation of the AsLOV2 Photoreceptor.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Effects of binding partners on thermal reversion rates of photoswitchable molecules.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

4 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Josiah P ZaynerDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, United States of America.
Tobin R SosnickDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois, United States of America ; Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois, United States of America.
University of Chicago · US

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Kinetic studies of protein foldingR01GM055694 · NIGMS · UNIVERSITY OF CHICAGO · PI SOSNICK, TOBIN R · 2001 to 2022
$7.6M
Spatial and temporal control of cell behavior with a genetically-encoded photoswiR01GM088668 · NIGMS · UNIVERSITY OF CHICAGO · PI GLOTZER, MICHAEL A., SOSNICK, TOBIN R · 2009 to 2012
$1.4M
NIGMS NIH HHS 5T32GM007183-34NIGMS NIH HHS GM088668NIGMS NIH HHS R01 GM055694NIGMS NIH HHS R01 GM088668NIGMS NIH HHS T32 GM007183
6 · The paper itself

Abstract

Algae, plants, bacteria and fungi contain Light-Oxygen-Voltage (LOV) domains that function as blue light sensors to control cellular responses to light. All LOV domains contain a bound flavin chromophore that is reduced upon photon absorption and forms a reversible, metastable covalent bond with a nearby cysteine residue. In Avena sativa LOV2 (AsLOV2), the photocycle is accompanied by an allosteric conformational change that activates the attached phototropin kinase in the full-length protein. Both the conformational change and formation of the cysteinyl-flavin adduct are stabilized by the reduction of the N5 atom in the flavin's isoalloxazine ring. In this study, we perform a mutational analysis to investigate the requirements for LOV2 to photocycle. We mutated all the residues that interact with the chromophore isoalloxazine ring to inert functional groups but none could fully inhibit the photocycle except those to the active-site cysteine. However, electronegative side chains in the vicinity of the chromophore accelerate the N5 deprotonation and the return to the dark state. Mutations to the N414 and Q513 residues identify a potential water gate and H₂O coordination sites. These residues affect the electronic nature of the chromophore and photocycle time by helping catalyze the N5 reduction leading to the completion of the photocycle. In addition, we demonstrate that dehydration leads to drastically slower photocycle times. Finally, to investigate the requirements of an active-site cysteine for photocycling, we moved the nearby cysteine to alternative locations and found that some variants can still photocycle. We propose a new model of the LOV domain photocycle that involves all of these components.

Indexed as

LightModels, MolecularAvenaCloning, MolecularDinitrocresolsDNA Mutational AnalysisImidazolesLight Signal TransductionMolecular StructureMutagenesis, Site-DirectedPlant ProteinsProtein Conformation4,6-dinitro-o-cresolDinitrocresolsimidazoleImidazolesPlant Proteins

Identifiers

PMID24475227
PMCPMC3903614
OpenAlexW1975563117

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.