The quorum-sensing protein TraR of Agrobacterium tumefaciens is susceptible to intrinsic and TraM-mediated proteolytic instability.

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 de

SUBMITTER: Costa ED 

PROVIDER: S-EPMC3359388 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature