Catabolism of Benzoate and Phthalate in
Rhodococcus
sp. Strain RHA1: Redundancies and Convergence
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Published:2005-06-15
Issue:12
Volume:187
Page:4050-4063
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ISSN:0021-9193
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Container-title:Journal of Bacteriology
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language:en
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Short-container-title:J Bacteriol
Author:
Patrauchan Marianna A.1, Florizone Christine1, Dosanjh Manisha1, Mohn William W.1, Davies Julian1, Eltis Lindsay D.1
Affiliation:
1. Department of Microbiology and Immunology, University of British Columbia, Vancouver, BC, V6T 1Z3, Canada
Abstract
ABSTRACT
Genomic and proteomic approaches were used to investigate phthalate and benzoate catabolism in
Rhodococcus
sp. strain RHA1, a polychlorinated biphenyl-degrading actinomycete. Sequence analyses identified genes involved in the catabolism of benzoate (
ben
) and phthalate (
pad
), the uptake of phthalate (
pat
), and two branches of the β-ketoadipate pathway (
catRABC
and
pcaJIHGBLFR
). The regulatory and structural
ben
genes are separated by genes encoding a cytochrome P450. The
pad
and
pat
genes are contained on a catabolic island that is duplicated on plasmids pRHL1 and pRHL2 and includes predicted terephthalate catabolic genes (
tpa
). Proteomic analyses demonstrated that the β-ketoadipate pathway is functionally convergent. Specifically, the
pad
and
pat
gene products were only detected in phthalate-grown cells. Similarly, the
ben
and
cat
gene products were only detected in benzoate-grown cells. However,
pca
-encoded enzymes were present under both growth conditions. Activity assays for key enzymes confirmed these results. Disruption of
pcaL
, which encodes a fusion enzyme, abolished growth on phthalate. In contrast, after a lag phase, growth of the mutant on benzoate was similar to that of the wild type. Proteomic analyses revealed 20 proteins in the mutant that were not detected in wild-type cells during growth on benzoate, including a CatD homolog that apparently compensated for loss of PcaL. Analysis of completed bacterial genomes indicates that the convergent β-ketoadipate pathway and some aspects of its genetic organization are characteristic of rhodococci and related actinomycetes. In contrast, the high redundancy of catabolic pathways and enzymes appears to be unique to RHA1 and may increase its potential to adapt to new carbon sources.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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