ArticleMolecular microbiology2012
The quorum-sensing protein TraR of Agrobacterium tumefaciens is susceptible to intrinsic and TraM-mediated proteolytic instability.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 21 citations in OpenAlex.
- Expanding the LuxR-type receptor functional repertoire: Protein-protein interactions in quorum sensing regulation.PLoS pathogens · 2026Review
- Investigation of the global translational response to oxidative stress in the model archaeonmSphere · 2025Article
- Insights into the Mechanisms of Small Molecule-Induced Agonism and Antagonism of a Quorum Sensing Receptor inJournal of the American Chemical Society · 2025Article
- Motility control through an anti-activation mechanism in Agrobacterium tumefaciens.Molecular microbiology · 2021Article
- Review
- Co-dependent and Interdigitated: Dual Quorum Sensing Systems Regulate Conjugative Transfer of the Ti Plasmid and the At Megaplasmid inFrontiers in microbiology · 2020Article
- The stress-related, rhizobial small RNA RcsR1 destabilizes the autoinducer synthase encoding mRNA sinI in Sinorhizobium meliloti.RNA biology · 2016Article
- Indole: a signaling molecule or a mere metabolic byproduct that alters bacterial physiology at a high concentration?Journal of microbiology (Seoul, Korea) · 2015Review
- RNase E affects the expression of the acyl-homoserine lactone synthase gene sinI in Sinorhizobium meliloti.Journal of bacteriology · 2014Article
- Profound impact of Hfq on nutrient acquisition, metabolism and motility in the plant pathogen Agrobacterium tumefaciens.PloS one · 2014Article
- Functions and regulation of quorum-sensing in Agrobacterium tumefaciens.Frontiers in plant science · 2014Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
TraR of Agrobacterium tumefaciens is a LuxR-type transcription factor that regulates genes required for replication and conjugation of the tumour-inducing plasmid. TraR binds the pheromone 3-oxo-octanoylhomoserine lactone (OOHL) and requires this molecule for folding into a protease-resistant, soluble conformation. Even after binding to OOHL, TraR is degraded at readily detectable rates. Here we show that the N-terminal domain of TraR, which binds OOHL, is more resistant to degradation than the full length protein, suggesting that sites on the C-terminal DNA binding domain [TraR(170-234)] enhance protein turnover. A fusion between GFP and TraR(170-234) was poorly fluorescent, and truncations of this fusion protein allowed us to identify residues in this domain that contribute to protein degradation. TraR activity was previously shown to be inhibited by the antiactivator TraM. These proteins form 2:2 complexes that fail to bind DNA sequences. Here we show that TraM sharply decreased the accumulation of TraR in whole cells, indicating that TraM facilitates proteolysis of TraR. The TraM component of these complexes is spared from proteolysis, and could therefore act catalytically.
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