ArticleThe Journal of biological chemistry2014
AccR is a master regulator involved in carbon catabolite repression of the anaerobic catabolism of aromatic compounds in Azoarcus sp. CIB.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 20 citations in OpenAlex.
- Differential anaerobic oxidation of benzoate inMicrobiology spectrum · 2025Article
- Further Insights into the Architecture of theGenes · 2019Article
- Article
- Transcriptional Regulation of the Peripheral Pathway for the Anaerobic Catabolism of Toluene andFrontiers in microbiology · 2018Article
- The Azoarcus anaerobius 1,3-Dihydroxybenzene (Resorcinol) Anaerobic Degradation Pathway Is Controlled by the Coordinated Activity of Two Enhancer-Binding Proteins.Applied and environmental microbiology · 2017Article
- Hierarchy of Carbon Source Utilization in Soil Bacteria: Hegemonic Preference for Benzoate in Complex Aromatic Compound Mixtures Degraded by Cupriavidus pinatubonensis Strain JMP134.Applied and environmental microbiology · 2015Article
- Unraveling the specific regulation of the central pathway for anaerobic degradation of 3-methylbenzoate.The Journal of biological chemistry · 2015Article
- Role of AcsR in expression of the acetyl-CoA synthetase gene in Vibrio vulnificus.BMC microbiology · 2015Article
- Benzoate mediates the simultaneous repression of anaerobic 4-methylbenzoate and succinate utilization in Magnetospirillum sp. strain pMbN1.BMC microbiology · 2014Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Here we characterized the first known transcriptional regulator that accounts for carbon catabolite repression (CCR) control of the anaerobic catabolism of aromatic compounds in bacteria. The AccR response regulator of Azoarcus sp. CIB controls succinate-responsive CCR of the central pathways for the anaerobic catabolism of aromatics by this strain. Phosphorylation of AccR to AccR-P triggers a monomer-to-dimer transition as well as the ability to bind to the target promoter and causes repression both in vivo and in vitro. Substitution of the Asp(60) phosphorylation target residue of the N-terminal receiver motif of AccR to a phosphomimic Glu residue generates a constitutively active derivative that behaves as a superrepressor of the target genes. AccR-P binds in vitro to a conserved inverted repeat (ATGCA-N6-TGCAT) present at two different locations within the PN promoter of the bzd genes for anaerobic benzoate degradation. Because the DNA binding-proficient C-terminal domain of AccR is monomeric, we propose an activation mechanism in which phosphorylation of Asp(60) of AccR alleviates interdomain repression mediated by the N-terminal domain. The presence of AccR-like proteins encoded in the genomes of other β-proteobacteria of the Azoarcus/Thauera group further suggests that AccR constitutes a master regulator that controls anaerobic CCR in these bacteria.
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