Impact of phenolic substrate and growth temperature on the Arthrobacter chlorophenolicus proteome.

We compared the Arthrobacter chlorophenolicus proteome during growth on 4-chlorophenol, 4-nitrophenol, or phenol at 5 and 28 degrees C, both for the wild-type and a mutant strain with mass spectrometry based proteomics. A label-free workflow employing spectral counting identified 3749 proteins across all growth conditions, representing over 70% of the predicted genome and 739 of these proteins form the core proteome. Statistically significant differences were found in the proteomes of cells grown under different conditions including differentiation of hundreds of unknown proteins.

Degradation of mixtures of phenolic compounds by Arthrobacter chlorophenolicus A6.

In this study the chlorophenol-degrading actinobacterium, Arthrobacter chlorophenolicus A6, was tested for its ability to grow on mixtures of phenolic compounds. During the experiments depletion of the compounds was monitored, as were cell growth and activity. Activity assays were based on bioluminescence output from a luciferase-tagged strain.

Adaptation of the psychrotroph Arthrobacter chlorophenolicus A6 to growth temperature and the presence of phenols by changes in the anteiso/iso ratio of branched fatty acids.

Arthrobacter chlorophenolicus is a previously described Gram-positive bacterium capable of degrading high concentrations of several phenolic compounds under optimal mesophilic (28 degrees C) as well as psychrophilic (5 degrees C) conditions. However, the exact mechanisms by which this organism is able to tolerate such extremes in temperature and high levels of toxic compounds are currently not known. In this study, we monitored changes in the fatty acid composition of the cell membrane under different extreme growth conditions.

Novel 4-chlorophenol degradation gene cluster and degradation route via hydroxyquinol in Arthrobacter chlorophenolicus A6.

Arthrobacter chlorophenolicus A6, a previously described 4-chlorophenol-degrading strain, was found to degrade 4-chlorophenol via hydroxyquinol, which is a novel route for aerobic microbial degradation of this compound. In addition, 10 open reading frames exhibiting sequence similarity to genes encoding enzymes involved in chlorophenol degradation were cloned and designated part of a chlorophenol degradation gene cluster (cph genes). Several of the open reading frames appeared to encode enzymes with similar functions; these open reading frames included two genes, cphA-I and cphA-II, which were shown to encode functional hydroxyquinol 1,2-dioxygenases.