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PhdA catalyzes the first step of phenazine-1-carboxylic acid degradation in Mycobacterium fortuitum

Costa, Kyle C. and Moskatel, Leon S. and Meirelles, Lucas A. and Newman, Dianne K. (2018) PhdA catalyzes the first step of phenazine-1-carboxylic acid degradation in Mycobacterium fortuitum. Journal of Bacteriology, 200 (10). Art. No. e00763-17. ISSN 0021-9193. PMCID PMC5915785. http://resolver.caltech.edu/CaltechAUTHORS:20180306-084603442

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Abstract

Phenazines are a class of bacterially produced redox-active metabolites that are found in natural, industrial, and clinical environments. In Pseudomonas spp., phenazine-1-carboxylic acid (PCA)—the precursor of all phenazine metabolites—facilitates nutrient acquisition, biofilm formation, and competition with other organisms. While the removal of phenazines negatively impacts these activities, little is known about the genes or enzymes responsible for phenazine degradation by other organisms. Here, we report that the first step of PCA degradation by Mycobacterium fortuitum is catalyzed by a phenazine-degrading decarboxylase (PhdA). PhdA is related to members of the UbiD protein family that rely on a prenylated flavin mononucleotide cofactor for activity. The gene for PhdB, the enzyme responsible for cofactor synthesis, is present in a putative operon with the gene encoding PhdA in a region of the M. fortuitum genome that is essential for PCA degradation. PhdA and PhdB are present in all known PCA-degrading organisms from the Actinobacteria. M. fortuitum can also catabolize other Pseudomonas-derived phenazines such as phenazine-1-carboxamide, 1-hydroxyphenazine, and pyocyanin. On the basis of our previous work and the current characterization of PhdA, we propose that degradation converges on a common intermediate: dihydroxyphenazine. An understanding of the genes responsible for degradation will enable targeted studies of phenazine degraders in diverse environments.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1128/JB.00763-17DOIArticle
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5915785/PubMed CentralArticle
ORCID:
AuthorORCID
Newman, Dianne K.0000-0003-1647-1918
Additional Information:© 2018 American Society for Microbiology. Received 18 December 2017. Accepted 16 February 2018. Accepted manuscript posted online 26 February 2018. We thank the members of the Newman lab for experimental advice and feedback on the manuscript. Grants to D.K.N. from the ARO (W911NF-17-1-0024) and NIH (1R01AI127850-01A1) supported this research. K.C.C. was supported by a Ruth L. Kirschstein National Research Service Award from the NIH, National Institute of Allergy and Infectious Diseases (grant no. F32AI112248).
Funders:
Funding AgencyGrant Number
Army Research Office (ARO)W911NF-17-1-0024
NIH1R01AI127850-01A1
NIH Predoctoral FellowshipF32AI112248
National Institute of Allergy and Infectious DiseasesUNSPECIFIED
Subject Keywords:mycobacteria, PCA, decarboxylases, degradation, phenazines
PubMed Central ID:PMC5915785
Record Number:CaltechAUTHORS:20180306-084603442
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:20180306-084603442
Official Citation:Costa KC, Moskatel LS, Meirelles LA, Newman DK. 2018. PhdA catalyzes the first step of phenazine-1-carboxylic acid degradation in Mycobacterium fortuitum. J Bacteriol 200:e00763-17. https://doi.org/10.1128/JB.00763-17.
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:85125
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:06 Mar 2018 17:49
Last Modified:02 Jan 2019 21:20

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