PMID:
     1522059
Authors:
     Dispensa M, Thomas CT, Kim MK, Perrotta JA, Gibson J, Harwood CS.
Title:
     Anaerobic growth of Rhodopseudomonas palustris on 4-hydroxybenzoate is dependent 
     on AadR, a member of the cyclic AMP receptor protein family of transcriptional
     regulators.
Journal:
     J Bacteriol. 1992 Sep;174(18):5803-13.
Abstract:
     The purple nonsulfur phototrophic bacterium Rhodopseudomonas palustris converts
     structurally diverse aromatic carboxylic acids, including lignin monomers, to
     benzoate and 4-hydroxybenzoate under anaerobic conditions. These compounds are
     then further degraded via aromatic ring-fission pathways. A gene termed aadR, for
     anaerobic aromatic degradation regulator, was identified by complementation of
     mutants unable to grow anaerobically on 4-hydroxybenzoate. The deduced amino acid
     sequence of the aadR product is similar to a family of transcriptional regulators
     which includes Escherichia coli Fnr and Crp, Pseudomonas aeruginosa Anr, and
     rhizobial FixK and FixK-like proteins. A mutant with a deletion in aadR failed to
     grow on 4-hydroxybenzoate under anaerobic conditions and grew very slowly on
     benzoate. It also did not express aromatic acid-coenzyme A ligase II, an enzyme
     that catalyzes the first step of 4-hydroxybenzoate degradation, and it was
     defective in 4-hydroxybenzoate-induced expression of benzoate-coenzyme A ligase. 
     The aadR deletion mutant was unaffected in other aspects of anaerobic growth. It 
     grew normally on nonaromatic carbon sources and also under nitrogen-fixing
     conditions. In addition, aerobic growth on 4-hydroxybenzoate was
     indistinguishable from that of the wild type. These results indicate that AadR
     functions as a transcriptional activator of anaerobic aromatic acid degradation.

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