Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics

Propionic acid (PA) is an important platform chemical in the food, agriculture, and pharmaceutical industries and is mainly biosynthesized by propionibacteria. Acid tolerance in PA-producing strains is crucial. In previous work, we investigated the acid tolerance mechanism of Propionibacterium acidi...

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Autores principales: Guan, Ningzi, Shin, Hyun-dong, Chen, Rachel R., Li, Jianghua, Liu, Long, Du, Guocheng, Chen, Jian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4223659/
https://www.ncbi.nlm.nih.gov/pubmed/25377721
http://dx.doi.org/10.1038/srep06951
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author Guan, Ningzi
Shin, Hyun-dong
Chen, Rachel R.
Li, Jianghua
Liu, Long
Du, Guocheng
Chen, Jian
author_facet Guan, Ningzi
Shin, Hyun-dong
Chen, Rachel R.
Li, Jianghua
Liu, Long
Du, Guocheng
Chen, Jian
author_sort Guan, Ningzi
collection PubMed
description Propionic acid (PA) is an important platform chemical in the food, agriculture, and pharmaceutical industries and is mainly biosynthesized by propionibacteria. Acid tolerance in PA-producing strains is crucial. In previous work, we investigated the acid tolerance mechanism of Propionibacterium acidipropionici at microenvironmental levels by analyzing physiological changes in the parental strain and three PA-tolerant mutants obtained by genome shuffling. However, the molecular mechanism of PA tolerance in P. acidipropionici remained unclear. Here, we performed a comparative proteomics study of P. acidipropionici CGMCC 1.2230 and the acid-tolerant mutant P. acidipropionici WSH1105; MALDI-TOF/MS identified 24 proteins that significantly differed between the parental and shuffled strains. The differentially expressed proteins were mainly categorized as key components of crucial biological processes and the acid stress response. Quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) was used to confirm differential expression of nine key proteins. Overexpression of the secretory protein glyceraldehyde-3-phosphate dehydrogenase and ATP synthase subunit α in Escherichia coli BL21 improved PA and acetic acid tolerance; overexpression of NADH dehydrogenase and methylmalonyl-CoA epimerase improved PA tolerance. These results provide new insights into the acid tolerance of P. acidipropionici and will facilitate the development of PA production through fermentation by propionibacteria.
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spelling pubmed-42236592014-11-13 Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics Guan, Ningzi Shin, Hyun-dong Chen, Rachel R. Li, Jianghua Liu, Long Du, Guocheng Chen, Jian Sci Rep Article Propionic acid (PA) is an important platform chemical in the food, agriculture, and pharmaceutical industries and is mainly biosynthesized by propionibacteria. Acid tolerance in PA-producing strains is crucial. In previous work, we investigated the acid tolerance mechanism of Propionibacterium acidipropionici at microenvironmental levels by analyzing physiological changes in the parental strain and three PA-tolerant mutants obtained by genome shuffling. However, the molecular mechanism of PA tolerance in P. acidipropionici remained unclear. Here, we performed a comparative proteomics study of P. acidipropionici CGMCC 1.2230 and the acid-tolerant mutant P. acidipropionici WSH1105; MALDI-TOF/MS identified 24 proteins that significantly differed between the parental and shuffled strains. The differentially expressed proteins were mainly categorized as key components of crucial biological processes and the acid stress response. Quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) was used to confirm differential expression of nine key proteins. Overexpression of the secretory protein glyceraldehyde-3-phosphate dehydrogenase and ATP synthase subunit α in Escherichia coli BL21 improved PA and acetic acid tolerance; overexpression of NADH dehydrogenase and methylmalonyl-CoA epimerase improved PA tolerance. These results provide new insights into the acid tolerance of P. acidipropionici and will facilitate the development of PA production through fermentation by propionibacteria. Nature Publishing Group 2014-11-07 /pmc/articles/PMC4223659/ /pubmed/25377721 http://dx.doi.org/10.1038/srep06951 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Guan, Ningzi
Shin, Hyun-dong
Chen, Rachel R.
Li, Jianghua
Liu, Long
Du, Guocheng
Chen, Jian
Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics
title Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics
title_full Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics
title_fullStr Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics
title_full_unstemmed Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics
title_short Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics
title_sort understanding of how propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4223659/
https://www.ncbi.nlm.nih.gov/pubmed/25377721
http://dx.doi.org/10.1038/srep06951
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