Evidence map›Paper›PMID 24019524›Full record

ArticleThe Journal of biological chemistry2013

Complex structure of the DNA-binding domain of AdpA, the global transcription factor in Streptomyces griseus, and a target duplex DNA reveals the structural basis of its tolerant DNA sequence specificity.

Ming Dong Yao, Jun Ohtsuka, Koji Nagata, Ken-Ichi Miyazono, Yuehua Zhi, Yasuo Ohnishi, Masaru Tanokura

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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

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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

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3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Article
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  5. A comparative metabologenomic approach reveals mechanistic insights intoProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  6. Article
  7. Article
  8. AdpAFrontiers in microbiology · 2019
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  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

7 authors.

Ming Dong YaoFrom the Departments of Applied Biological Chemistry and.
Jun Ohtsuka
Koji Nagata
Ken-Ichi Miyazono
Yuehua Zhi
Yasuo Ohnishi
Masaru Tanokura

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

AdpA serves as the global transcription factor in the A-factor regulatory cascade, controlling the secondary metabolism and morphological differentiation of the filamentous bacterium Streptomyces griseus. AdpA binds to over 500 operator regions with the consensus sequence 5'-TGGCSNGWWY-3' (where S is G or C, W is A or T, Y is T or C, and N is any nucleotide). However, it is still obscure how AdpA can control hundreds of genes. To elucidate the structural basis of this tolerant DNA recognition by AdpA, we focused on the interaction between the DNA-binding domain of AdpA (AdpA-DBD), which consists of two helix-turn-helix motifs, and a target duplex DNA containing the consensus sequence 5'-TGGCGGGTTC-3'. The crystal structure of the AdpA-DBD-DNA complex and the mutant analysis of AdpA-DBD revealed its unique manner of DNA recognition, whereby only two arginine residues directly recognize the consensus sequence, explaining the strict recognition of G and C at positions 2 and 4, respectively, and the tolerant recognition of other positions of the consensus sequence. AdpA-DBD confers tolerant DNA sequence specificity to AdpA, allowing it to control hundreds of genes as a global transcription factor.

Indexed as

Response ElementsBacterial ProteinsCrystallography, X-RayDNA, BacterialProtein Structure, TertiaryStreptomyces griseusTrans-ActivatorsAdpA protein, Streptomyces griseusBacterial ProteinsDNA, BacterialTrans-ActivatorsAdpAA-factorDNA-binding DomainDNA-binding ProteinDNA-Protein InteractionDNA Sequence SpecificityDNA StructureGlobal Transcription FactorTranscription FactorsX-ray Crystallography

Identifiers

PMID24019524
PMCPMC3829415

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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.