ArticleThe Journal of biological chemistry2011
The Agrobacterium tumefaciens transcription factor BlcR is regulated via oligomerization.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Untangling the Complexity of Two-Component Signal Transduction in Bacteria.Microorganisms · 2025Review
- Thermal shift assay to identify ligands for bacterial sensor proteins.FEMS microbiology reviews · 2025Review
- Unveiling the regulatory mechanisms of salicylate degradation gene clusterApplied and environmental microbiology · 2023Article
- A sweet new set of inducible and constitutive promoters inFrontiers in microbiology · 2023Article
- A paper-based, cell-free biosensor system for the detection of heavy metals and date rape drugs.PloS one · 2019Article
- Succinic Semialdehyde Promotes Prosurvival Capability of Agrobacterium tumefaciens.Journal of bacteriology · 2016Article
- D101 is critical for the function of AttJ, a repressor of quorum quenching system in Agrobacterium tumefaciens.Journal of microbiology (Seoul, Korea) · 2015Article
- In vivo analysis of DNA binding and ligand interaction of BlcR, an IclR-type repressor from Agrobacterium tumefaciens.Microbiology (Reading, England) · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The Agrobacterium tumefaciens BlcR is a member of the emerging isocitrate lyase transcription regulators that negatively regulates metabolism of γ-butyrolactone, and its repressing function is relieved by succinate semialdehyde (SSA). Our crystal structure showed that BlcR folded into the DNA- and SSA-binding domains and dimerized via the DNA-binding domains. Mutational analysis identified residues, including Phe(147), that are important for SSA association; BlcR(F147A) existed as tetramer. Two BlcR dimers bound to target DNA and in a cooperative manner, and the distance between the two BlcR-binding sequences in DNA was critical for BlcR-DNA association. Tetrameric BlcR(F147A) retained DNA binding activity, and importantly, this activity was not affected by the distance separating the BlcR-binding sequences in DNA. SSA did not dissociate tetrameric BlcR(F147A) or BlcR(F147A)-DNA. As well as in the SSA-binding site, Phe(147) is located in a structurally flexible loop that may be involved in BlcR oligomerization. We propose that SSA regulates BlcR DNA-binding function via oligomerization.
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Registered trials
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.