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Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440

Glutarate, a metabolic intermediate in the catabolism of several amino acids and aromatic compounds, can be catabolized through both the glutarate hydroxylation pathway and the glutaryl-coenzyme A (glutaryl-CoA) dehydrogenation pathway in Pseudomonas putida KT2440. The elucidation of the regulatory...

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Autores principales: Zhang, Manman, Kang, Zhaoqi, Guo, Xiaoting, Guo, Shiting, Xiao, Dan, Liu, Yidong, Ma, Cuiqing, Gao, Chao, Xu, Ping
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6667623/
https://www.ncbi.nlm.nih.gov/pubmed/31363033
http://dx.doi.org/10.1128/mBio.01570-19
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author Zhang, Manman
Kang, Zhaoqi
Guo, Xiaoting
Guo, Shiting
Xiao, Dan
Liu, Yidong
Ma, Cuiqing
Gao, Chao
Xu, Ping
author_facet Zhang, Manman
Kang, Zhaoqi
Guo, Xiaoting
Guo, Shiting
Xiao, Dan
Liu, Yidong
Ma, Cuiqing
Gao, Chao
Xu, Ping
author_sort Zhang, Manman
collection PubMed
description Glutarate, a metabolic intermediate in the catabolism of several amino acids and aromatic compounds, can be catabolized through both the glutarate hydroxylation pathway and the glutaryl-coenzyme A (glutaryl-CoA) dehydrogenation pathway in Pseudomonas putida KT2440. The elucidation of the regulatory mechanism could greatly aid in the design of biotechnological alternatives for glutarate production. In this study, it was found that a GntR family protein, CsiR, and a LysR family protein, GcdR, regulate the catabolism of glutarate by repressing the transcription of csiD and lhgO, two key genes in the glutarate hydroxylation pathway, and by activating the transcription of gcdH and gcoT, two key genes in the glutaryl-CoA dehydrogenation pathway, respectively. Our data suggest that CsiR and GcdR are independent and that there is no cross-regulation between the two pathways. l-2-Hydroxyglutarate (l-2-HG), a metabolic intermediate in the glutarate catabolism with various physiological functions, has never been elucidated in terms of its metabolic regulation. Here, we reveal that two molecules, glutarate and l-2-HG, act as effectors of CsiR and that P. putida KT2440 uses CsiR to sense glutarate and l-2-HG and to utilize them effectively. This report broadens our understanding of the bacterial regulatory mechanisms of glutarate and l-2-HG catabolism and may help to identify regulators of l-2-HG catabolism in other species.
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spelling pubmed-66676232019-08-06 Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440 Zhang, Manman Kang, Zhaoqi Guo, Xiaoting Guo, Shiting Xiao, Dan Liu, Yidong Ma, Cuiqing Gao, Chao Xu, Ping mBio Research Article Glutarate, a metabolic intermediate in the catabolism of several amino acids and aromatic compounds, can be catabolized through both the glutarate hydroxylation pathway and the glutaryl-coenzyme A (glutaryl-CoA) dehydrogenation pathway in Pseudomonas putida KT2440. The elucidation of the regulatory mechanism could greatly aid in the design of biotechnological alternatives for glutarate production. In this study, it was found that a GntR family protein, CsiR, and a LysR family protein, GcdR, regulate the catabolism of glutarate by repressing the transcription of csiD and lhgO, two key genes in the glutarate hydroxylation pathway, and by activating the transcription of gcdH and gcoT, two key genes in the glutaryl-CoA dehydrogenation pathway, respectively. Our data suggest that CsiR and GcdR are independent and that there is no cross-regulation between the two pathways. l-2-Hydroxyglutarate (l-2-HG), a metabolic intermediate in the glutarate catabolism with various physiological functions, has never been elucidated in terms of its metabolic regulation. Here, we reveal that two molecules, glutarate and l-2-HG, act as effectors of CsiR and that P. putida KT2440 uses CsiR to sense glutarate and l-2-HG and to utilize them effectively. This report broadens our understanding of the bacterial regulatory mechanisms of glutarate and l-2-HG catabolism and may help to identify regulators of l-2-HG catabolism in other species. American Society for Microbiology 2019-07-30 /pmc/articles/PMC6667623/ /pubmed/31363033 http://dx.doi.org/10.1128/mBio.01570-19 Text en Copyright © 2019 Zhang et al. https://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Research Article
Zhang, Manman
Kang, Zhaoqi
Guo, Xiaoting
Guo, Shiting
Xiao, Dan
Liu, Yidong
Ma, Cuiqing
Gao, Chao
Xu, Ping
Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440
title Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440
title_full Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440
title_fullStr Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440
title_full_unstemmed Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440
title_short Regulation of Glutarate Catabolism by GntR Family Regulator CsiR and LysR Family Regulator GcdR in Pseudomonas putida KT2440
title_sort regulation of glutarate catabolism by gntr family regulator csir and lysr family regulator gcdr in pseudomonas putida kt2440
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6667623/
https://www.ncbi.nlm.nih.gov/pubmed/31363033
http://dx.doi.org/10.1128/mBio.01570-19
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