Evidence map›Paper›PMID 27129205›Full record

ArticleThe Journal of biological chemistry2016

How Aromatic Compounds Block DNA Binding of HcaR Catabolite Regulator.

Youngchang Kim, Grazyna Joachimiak, Lance Bigelow, Gyorgy Babnigg, Andrzej Joachimiak

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. A Dual-Receptor System MediatesJournal of agricultural and food chemistry · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Genomic analysis ofBiotechnology for biofuels · 2019
    Article
  13. Article
  14. Article
  15. Review
  16. Regulation of Metabolic Pathways by MarR Family Transcription Factors.Computational and structural biotechnology journal · 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

5 authors at 1 institution in 1 country.

Youngchang KimFrom the Midwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, Illinois 60439.
Grazyna JoachimiakFrom the Midwest Center for Structural Genomics and.
Lance BigelowFrom the Midwest Center for Structural Genomics and.
Gyorgy BabniggFrom the Midwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, Illinois 60439.
Andrzej JoachimiakFrom the Midwest Center for Structural Genomics and Structural Biology Center, Biosciences, Argonne National Laboratory, Argonne, Illinois 60439 andrzejj@anl.gov.
Argonne National Laboratory · US

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI OTWINOWSKI, ZBYSZEK · 2010 to 2014
$33.7M
The Midwest Center for Structural Genomics - Community ResourceR24GM115586 · NIGMS · UNIVERSITY OF CHICAGO · PI JOACHIMIAK, ANDRZEJ · 2015 to 2017
$2.8M
NIGMS NIH HHS R24 GM115586NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

Bacterial catabolism of aromatic compounds from various sources including phenylpropanoids and flavonoids that are abundant in soil plays an important role in the recycling of carbon in the ecosystem. We have determined the crystal structures of apo-HcaR from Acinetobacter sp. ADP1, a MarR/SlyA transcription factor, in complexes with hydroxycinnamates and a specific DNA operator. The protein regulates the expression of the hca catabolic operon in Acinetobacter and related bacterial strains, allowing utilization of hydroxycinnamates as sole sources of carbon. HcaR binds multiple ligands, and as a result the transcription of genes encoding several catabolic enzymes is increased. The 1.9-2.4 Å resolution structures presented here explain how HcaR recognizes four ligands (ferulate, 3,4-dihydroxybenzoate, p-coumarate, and vanillin) using the same binding site. The ligand promiscuity appears to be an adaptation to match a broad specificity of hydroxycinnamate catabolic enzymes while responding to toxic thioester intermediates. Structures of apo-HcaR and in complex with a specific DNA hca operator when combined with binding studies of hydroxycinnamates show how aromatic ligands render HcaR unproductive in recognizing a specific DNA target. The current study contributes to a better understanding of the hca catabolic operon regulation mechanism by the transcription factor HcaR.

Indexed as

AcinetobacterAmino Acid SequenceBacterial ProteinsBinding SitesConserved SequenceCoumaric AcidsCrystallography, X-RayDNA, BacterialGene Expression Regulation, BacterialModels, MolecularMolecular Sequence DataProtein BindingProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryTranscription FactorsBacterial ProteinsCoumaric AcidsDNA, Bacterialferulic acidTranscription Factorsarabinose utilizationbacterial transcriptionDNA bindingDNA-binding proteinhuman gut bacterialigand-binding proteinligand-induced conformational changemetabolic regulationNUDIX familyprotein conformation

Identifiers

PMID27129205
PMCPMC4933237
OpenAlexW2344410986

What OpenQuestion holds

Textmetadata
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.