Evidence map›Paper›PMID 22170053›Full record

ArticleThe Journal of biological chemistry2012

Eukaryotic class II cyclobutane pyrimidine dimer photolyase structure reveals basis for improved ultraviolet tolerance in plants.

Kenichi Hitomi, Andrew S Arvai, Junpei Yamamoto, Chiharu Hitomi, Mika Teranishi, Tokuhisa Hirouchi, Kazuo Yamamoto, Shigenori Iwai, John A Tainer, Jun Hidema and 1 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed, 1 pooled it
–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

19 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Elucidation of a distinct photoreduction pathway in class IIProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Photolyase: Dynamics and electron-transfer mechanisms of DNA repair.Archives of biochemistry and biophysics · 2017
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. DNA repair by reversal of DNA damage.Cold Spring Harbor perspectives in biology · 2013
    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

11 authors.

Kenichi HitomiGraduate School of Engineering Science, Osaka University, Machikaneyama-cho 1-3, Toyonaka, Osaka 560-8531, Japan.
Andrew S Arvai
Junpei Yamamoto
Chiharu Hitomi
Mika Teranishi
Tokuhisa Hirouchi
Kazuo Yamamoto
Shigenori Iwai
John A Tainer
Jun Hidema
Elizabeth D Getzoff

Funding

STRUCTURE AND FUNCTION OF METALLOENZYMES FOR DNA REPAIRR01GM046312 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI TAINER, JOHN A. · 1991 to 2012
$5.9M
STRUCTURAL ANALYSIS OF CHROMATICALLY ACTIVE PROTEINSR01GM037684 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GETZOFF, ELIZABETH D · 1987 to 2009
$3.1M
NIGMS NIH HHS GM046312NIGMS NIH HHS GM37684NIGMS NIH HHS R01 GM037684NIGMS NIH HHS R01 GM046312
6 · The paper itself

Abstract

Ozone depletion increases terrestrial solar ultraviolet B (UV-B; 280-315 nm) radiation, intensifying the risks plants face from DNA damage, especially covalent cyclobutane pyrimidine dimers (CPD). Without efficient repair, UV-B destroys genetic integrity, but plant breeding creates rice cultivars with more robust photolyase (PHR) DNA repair activity as an environmental adaptation. So improved strains of Oryza sativa (rice), the staple food for Asia, have expanded rice cultivation worldwide. Efficient light-driven PHR enzymes restore normal pyrimidines to UV-damaged DNA by using blue light via flavin adenine dinucleotide to break pyrimidine dimers. Eukaryotes duplicated the photolyase gene, producing PHRs that gained functions and adopted activities that are distinct from those of prokaryotic PHRs yet are incompletely understood. Many multicellular organisms have two types of PHR: (6-4) PHR, which structurally resembles bacterial CPD PHRs but recognizes different substrates, and Class II CPD PHR, which is remarkably dissimilar in sequence from bacterial PHRs despite their common substrate. To understand the enigmatic DNA repair mechanisms of PHRs in eukaryotic cells, we determined the first crystal structure of a eukaryotic Class II CPD PHR from the rice cultivar Sasanishiki. Our 1.7 Å resolution PHR structure reveals structure-activity relationships in Class II PHRs and tuning for enhanced UV tolerance in plants. Structural comparisons with prokaryotic Class I CPD PHRs identified differences in the binding site for UV-damaged DNA substrate. Convergent evolution of both flavin hydrogen bonding and a Trp electron transfer pathway establish these as critical functional features for PHRs. These results provide a paradigm for light-dependent DNA repair in higher organisms.

Indexed as

Amino Acid MotifsBase SequenceBinding SitesCatalytic DomainCrystallography, X-RayDeoxyribodipyrimidine Photo-LyaseDNADNA RepairElectrophoretic Mobility Shift AssayFlavin-Adenine DinucleotideHydrogen BondingMolecular Sequence DataNucleic Acid ConformationOryzaPhosphorylationPhylogenyDeoxyribodipyrimidine Photo-LyaseDNAFlavin-Adenine DinucleotidePlant Proteins

Identifiers

PMID22170053
PMCPMC3320952

What OpenQuestion holds

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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.