Evidence map›Paper›PMID 25550425›Full record

ArticleNucleic acids research2015

Structural basis of DNA recognition by PCG2 reveals a novel DNA binding mode for winged helix-turn-helix domains.

Junfeng Liu, Jinguang Huang, Yanxiang Zhao, Huaian Liu, Dawei Wang, Jun Yang, Wensheng Zhao, Ian A Taylor, You-Liang Peng

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. 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

9 authors at 2 institutions in 1 country.

Junfeng LiuMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China.
Jinguang HuangMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China State key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao, Shandong 266109, China.
Yanxiang ZhaoMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China.
Huaian LiuMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China.
Dawei WangMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China State key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
Jun YangMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China State key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
Wensheng ZhaoMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China State key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China.
Ian A TaylorDivision of Molecular Structure, MRC-NIMR, London, NW7 1AA, UK.
You-Liang PengMOA Key Laboratory of Plant Pathology, China Agricultural University, Beijing 100193, China State key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, China pengyl@cau.edu.cn.
China Agricultural University · CNQingdao Agricultural University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The MBP1 family proteins are the DNA binding subunits of MBF cell-cycle transcription factor complexes and contain an N terminal winged helix-turn-helix (wHTH) DNA binding domain (DBD). Although the DNA binding mechanism of MBP1 from Saccharomyces cerevisiae has been extensively studied, the structural framework and the DNA binding mode of other MBP1 family proteins remains to be disclosed. Here, we determined the crystal structure of the DBD of PCG2, the Magnaporthe oryzae orthologue of MBP1, bound to MCB-DNA. The structure revealed that the wing, the 20-loop, helix A and helix B in PCG2-DBD are important elements for DNA binding. Unlike previously characterized wHTH proteins, PCG2-DBD utilizes the wing and helix-B to bind the minor groove and the major groove of the MCB-DNA whilst the 20-loop and helix A interact non-specifically with DNA. Notably, two glutamines Q89 and Q82 within the wing were found to recognize the MCB core CGCG sequence through making hydrogen bond interactions. Further in vitro assays confirmed essential roles of Q89 and Q82 in the DNA binding. These data together indicate that the MBP1 homologue PCG2 employs an unusual mode of binding to target DNA and demonstrate the versatility of wHTH domains.

Indexed as

DNADNA-Binding ProteinsHelix-Turn-Helix MotifsMagnaportheModels, MolecularProtein BindingDNADNA-Binding Proteins

Identifiers

PMID25550425
PMCPMC4333399
OpenAlexW2166757507

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.