Evidence map›Paper›PMID 26065359›Full record

ArticleNature communications2015

The molecular origin of high DNA-repair efficiency by photolyase.

Chuang Tan, Zheyun Liu, Jiang Li, Xunmin Guo, Lijuan Wang, Aziz Sancar, Dongping Zhong

Open access · goldAbstract read
PubMed Publisher
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
12.9field-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

25 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
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  8. Article
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  14. Article
  15. Theoretical insights into the DNA repair function ofBiophysics and physicobiology · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. A DNA-Based Magnetic Sensor.ACS central science · 2018
    Article
  20. Photolyase: Dynamics and electron-transfer mechanisms of DNA repair.Archives of biochemistry and biophysics · 2017
    Review
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 2 institutions in 1 country.

Chuang TanDepartment of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Zheyun LiuDepartment of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Jiang LiDepartment of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Xunmin GuoDepartment of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Lijuan WangDepartment of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
Aziz SancarDepartment of Biochemistry and Biophysics, University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599, USA.
Dongping ZhongDepartment of Physics, Department of Chemistry and Biochemistry, and Programs of Biophysics, Chemical Physics, and Biochemistry, The Ohio State University, Columbus, Ohio 43210, USA.
The Ohio State University · USUniversity of North Carolina at Chapel Hill · US

Funding

STRUCTURE/FUNCTION OF DNA PHOTOLYASER01GM031082 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI SANCAR, AZIZ · 1985 to 2015
$4.9M
STRUCTURE/FUNCTION OF DNA PHOTOLYASER37GM031082 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI SANCAR, AZIZ · 1995 to 2004
$2.6M
Functional Dynamics and Molecular Mechanism of PhotolayseR01GM074813 · NIGMS · OHIO STATE UNIVERSITY · PI ZHONG, DONGPING · 2007 to 2016
$2.6M
NIGMS NIH HHS GM074813NIGMS NIH HHS GM31082
6 · The paper itself

Abstract

The primary dynamics in photomachinery such as charge separation in photosynthesis and bond isomerization in sensory photoreceptor are typically ultrafast to accelerate functional dynamics and avoid energy dissipation. The same is also true for the DNA repair enzyme, photolyase. However, it is not known how the photoinduced step is optimized in photolyase to attain maximum efficiency. Here, we analyse the primary reaction steps of repair of ultraviolet-damaged DNA by photolyase using femtosecond spectroscopy. With systematic mutations of the amino acids involved in binding of the flavin cofactor and the cyclobutane pyrimidine dimer substrate, we report our direct deconvolution of the catalytic dynamics with three electron-transfer and two bond-breaking elementary steps and thus the fine tuning of the biological repair function for optimal efficiency. We found that the maximum repair efficiency is not enhanced by the ultrafast photoinduced process but achieved by the synergistic optimization of all steps in the complex repair reaction.

Indexed as

DNA RepairBiocatalysisCatalytic DomainDeoxyribodipyrimidine Photo-LyaseMutationDeoxyribodipyrimidine Photo-Lyase

Identifiers

PMID26065359
OpenAlexW2257280499

What OpenQuestion holds

Textmetadata
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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.