Evidence map›Paper›PMID 35013256›Full record

ArticleNature communications2022

Dynamics and mechanism of dimer dissociation of photoreceptor UVR8.

Xiankun Li, Zheyun Liu, Haisheng Ren, Mainak Kundu, Frank W Zhong, Lijuan Wang, Jiali Gao, Dongping Zhong

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Excimer Energies.The journal of physical chemistry letters · 2023
    Article
  11. Article
  12. Review
  13. 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

8 authors.

Xiankun LiDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.ORCID 0000-0002-5022-8172
Zheyun LiuDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.
Haisheng RenDepartment of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, MN, 55455, USA.ORCID 0000-0002-8638-7570
Mainak KunduDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.
Frank W ZhongCell and Molecular Biology Program, University of Chicago, Chicago, IL, 60637, USA.
Lijuan WangDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA.
Jiali GaoDepartment of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, MN, 55455, USA. jiali@jialigao.org.ORCID 0000-0003-0106-7154
Dongping ZhongDepartment of Physics, Department of Chemistry and Biochemistry, Programs of Biophysics, Chemical Physics and Biochemistry, The Ohio State University, Columbus, OH, 43210, USA. zhong.28@osu.edu.ORCID 0000-0001-9381-8992

Funding

BIOMOLECULAR INTERACTIONS AND ENZYMATIC PROCESSESR01GM046736 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI JIALI GAO · 1993 to 2026
$6.5M
Biological dynamics for protein properties and functionsR35GM144047 · NIGMS · OHIO STATE UNIVERSITY · PI ZHONG, DONGPING · 2022 to 2023
$934k
NIGMS NIH HHS R01 GM046736NIGMS NIH HHS R35 GM144047
6 · The paper itself

Abstract

Photoreceptors are a class of light-sensing proteins with critical biological functions. UVR8 is the only identified UV photoreceptor in plants and its dimer dissociation upon UV sensing activates UV-protective processes. However, the dissociation mechanism is still poorly understood. Here, by integrating extensive mutations, ultrafast spectroscopy, and computational calculations, we find that the funneled excitation energy in the interfacial tryptophan (Trp) pyramid center drives a directional Trp-Trp charge separation in 80 ps and produces a critical transient Trp anion, enabling its ultrafast charge neutralization with a nearby positive arginine residue in 17 ps to destroy a key salt bridge. A domino effect is then triggered to unzip the strong interfacial interactions, which is facilitated through flooding the interface by channel and interfacial water molecules. These detailed dynamics reveal a unique molecular mechanism of UV-induced dimer monomerization.

Indexed as

AnionsArabidopsisArabidopsis ProteinsArginineBinding SitesChromosomal Proteins, Non-HistoneCloning, MolecularEscherichia coliGene ExpressionGenetic VectorsKineticsMolecular Dynamics SimulationMutationProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandAnionsArabidopsis ProteinsArginineChromosomal Proteins, Non-HistoneRecombinant ProteinsTryptophanUvr8 protein, ArabidopsisWater

Identifiers

PMID35013256
PMCPMC8748919

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Registered trials

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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.