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Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition
Zymomonas mobilis, a promising candidate for industrial biofuel production, is capable of nitrogen fixation naturally without hindering ethanol production. However, little is known about the regulation of nitrogen fixation in Z. mobilis. We herein conducted a high throughput analysis of proteome and...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8600466/ https://www.ncbi.nlm.nih.gov/pubmed/34803957 http://dx.doi.org/10.3389/fmicb.2021.740555 |
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author | Nisar, Ayesha Gongye, Xiangxu Huang, Yuhuan Khan, Sawar Chen, Mao Wu, Bo He, Mingxiong |
author_facet | Nisar, Ayesha Gongye, Xiangxu Huang, Yuhuan Khan, Sawar Chen, Mao Wu, Bo He, Mingxiong |
author_sort | Nisar, Ayesha |
collection | PubMed |
description | Zymomonas mobilis, a promising candidate for industrial biofuel production, is capable of nitrogen fixation naturally without hindering ethanol production. However, little is known about the regulation of nitrogen fixation in Z. mobilis. We herein conducted a high throughput analysis of proteome and protein acetylation in Z. mobilis under N(2)-fixing conditions and established its first acetylome. The upregulated proteins mainly belong to processes of nitrogen fixation, motility, chemotaxis, flagellar assembly, energy production, transportation, and oxidation–reduction. Whereas, downregulated proteins are mainly related to energy-consuming and biosynthetic processes. Our acetylome analyses revealed 197 uniquely acetylated proteins, belonging to major pathways such as nitrogen fixation, central carbon metabolism, ammonia assimilation pathway, protein biosynthesis, and amino acid metabolism. Further, we observed acetylation in glycolytic enzymes of central carbon metabolism, the nitrogenase complex, the master regulator NifA, and the enzyme in GS/GOGAT cycle. These findings suggest that protein acetylation may play an important role in regulating various aspects of N(2)-metabolism in Z. mobilis. This study provides new knowledge of specific proteins and their associated cellular processes and pathways that may be regulated by protein acetylation in Z. mobilis. |
format | Online Article Text |
id | pubmed-8600466 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-86004662021-11-19 Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition Nisar, Ayesha Gongye, Xiangxu Huang, Yuhuan Khan, Sawar Chen, Mao Wu, Bo He, Mingxiong Front Microbiol Microbiology Zymomonas mobilis, a promising candidate for industrial biofuel production, is capable of nitrogen fixation naturally without hindering ethanol production. However, little is known about the regulation of nitrogen fixation in Z. mobilis. We herein conducted a high throughput analysis of proteome and protein acetylation in Z. mobilis under N(2)-fixing conditions and established its first acetylome. The upregulated proteins mainly belong to processes of nitrogen fixation, motility, chemotaxis, flagellar assembly, energy production, transportation, and oxidation–reduction. Whereas, downregulated proteins are mainly related to energy-consuming and biosynthetic processes. Our acetylome analyses revealed 197 uniquely acetylated proteins, belonging to major pathways such as nitrogen fixation, central carbon metabolism, ammonia assimilation pathway, protein biosynthesis, and amino acid metabolism. Further, we observed acetylation in glycolytic enzymes of central carbon metabolism, the nitrogenase complex, the master regulator NifA, and the enzyme in GS/GOGAT cycle. These findings suggest that protein acetylation may play an important role in regulating various aspects of N(2)-metabolism in Z. mobilis. This study provides new knowledge of specific proteins and their associated cellular processes and pathways that may be regulated by protein acetylation in Z. mobilis. Frontiers Media S.A. 2021-10-07 /pmc/articles/PMC8600466/ /pubmed/34803957 http://dx.doi.org/10.3389/fmicb.2021.740555 Text en Copyright © 2021 Nisar, Gongye, Huang, Khan, Chen, Wu and He. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Nisar, Ayesha Gongye, Xiangxu Huang, Yuhuan Khan, Sawar Chen, Mao Wu, Bo He, Mingxiong Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition |
title | Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition |
title_full | Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition |
title_fullStr | Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition |
title_full_unstemmed | Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition |
title_short | Genome-Wide Analyses of Proteome and Acetylome in Zymomonas mobilis Under N(2)-Fixing Condition |
title_sort | genome-wide analyses of proteome and acetylome in zymomonas mobilis under n(2)-fixing condition |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8600466/ https://www.ncbi.nlm.nih.gov/pubmed/34803957 http://dx.doi.org/10.3389/fmicb.2021.740555 |
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