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Systematic analysis of lysine malonylation in Streptococcus mutans
Protein lysine malonylation (Kmal) is a novel post-translational modification (PTM) that regulates various biological pathways such as energy metabolism and translation. Malonylation in prokaryotes, however, is still poorly understood. In this study, we performed a global Kmal analysis of the cariog...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9742479/ https://www.ncbi.nlm.nih.gov/pubmed/36519128 http://dx.doi.org/10.3389/fcimb.2022.1078572 |
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author | Li, Zhengyi Wu, Qinrui Zhang, Yixin Zhou, Xuedong Peng, Xian |
author_facet | Li, Zhengyi Wu, Qinrui Zhang, Yixin Zhou, Xuedong Peng, Xian |
author_sort | Li, Zhengyi |
collection | PubMed |
description | Protein lysine malonylation (Kmal) is a novel post-translational modification (PTM) that regulates various biological pathways such as energy metabolism and translation. Malonylation in prokaryotes, however, is still poorly understood. In this study, we performed a global Kmal analysis of the cariogenic organism Streptococcus mutans by combining antibody-based affinity enrichment and high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) analysis. Altogether, 392 malonyllysine sites in 159 proteins were identified. Subsequent bioinformatic analysis revealed that Kmal occurs in proteins involved in various metabolic pathways including translation machinery, energy metabolism, RNA degradation, and biosynthesis of various secondary metabolites. Quantitative analysis demonstrated that Kmal substrates were globally altered in the biofilm growth state compared to the planktonic growth state. Furthermore, a comparative analysis of the lysine malonylome of our study with previously determined lysine acetylome in S. mutans revealed that a small proportion of Kmal sites overlapped with acetylated sites, whereby suggesting that these two acylations have distinct functional implications. These results expand our knowledge of Kmal in prokaryotes, providing a resource for researching metabolic regulation of bacterial virulence and physiological functions by PTM. |
format | Online Article Text |
id | pubmed-9742479 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-97424792022-12-13 Systematic analysis of lysine malonylation in Streptococcus mutans Li, Zhengyi Wu, Qinrui Zhang, Yixin Zhou, Xuedong Peng, Xian Front Cell Infect Microbiol Cellular and Infection Microbiology Protein lysine malonylation (Kmal) is a novel post-translational modification (PTM) that regulates various biological pathways such as energy metabolism and translation. Malonylation in prokaryotes, however, is still poorly understood. In this study, we performed a global Kmal analysis of the cariogenic organism Streptococcus mutans by combining antibody-based affinity enrichment and high-performance liquid chromatography-tandem mass spectrometry (HPLC-MS/MS) analysis. Altogether, 392 malonyllysine sites in 159 proteins were identified. Subsequent bioinformatic analysis revealed that Kmal occurs in proteins involved in various metabolic pathways including translation machinery, energy metabolism, RNA degradation, and biosynthesis of various secondary metabolites. Quantitative analysis demonstrated that Kmal substrates were globally altered in the biofilm growth state compared to the planktonic growth state. Furthermore, a comparative analysis of the lysine malonylome of our study with previously determined lysine acetylome in S. mutans revealed that a small proportion of Kmal sites overlapped with acetylated sites, whereby suggesting that these two acylations have distinct functional implications. These results expand our knowledge of Kmal in prokaryotes, providing a resource for researching metabolic regulation of bacterial virulence and physiological functions by PTM. Frontiers Media S.A. 2022-11-28 /pmc/articles/PMC9742479/ /pubmed/36519128 http://dx.doi.org/10.3389/fcimb.2022.1078572 Text en Copyright © 2022 Li, Wu, Zhang, Zhou and Peng 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 | Cellular and Infection Microbiology Li, Zhengyi Wu, Qinrui Zhang, Yixin Zhou, Xuedong Peng, Xian Systematic analysis of lysine malonylation in Streptococcus mutans |
title | Systematic analysis of lysine malonylation in Streptococcus mutans
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title_full | Systematic analysis of lysine malonylation in Streptococcus mutans
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title_fullStr | Systematic analysis of lysine malonylation in Streptococcus mutans
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title_full_unstemmed | Systematic analysis of lysine malonylation in Streptococcus mutans
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title_short | Systematic analysis of lysine malonylation in Streptococcus mutans
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title_sort | systematic analysis of lysine malonylation in streptococcus mutans |
topic | Cellular and Infection Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9742479/ https://www.ncbi.nlm.nih.gov/pubmed/36519128 http://dx.doi.org/10.3389/fcimb.2022.1078572 |
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