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Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways

Lysine acylations are reversible and ubiquitous post-translational modifications that play critical roles in regulating multiple cellular processes. In the current study, highly abundant and dynamic acetylation, besides succinylation, was uncovered in a soil bacterium, Streptomyces coelicolor. By af...

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Autores principales: Yang, Yujiao, Zhang, Hong, Guo, Zhenyang, Zou, Siwei, Long, Fei, Wu, Jiacheng, Li, Peng, Zhao, Guo-ping, Zhao, Wei
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8498004/
https://www.ncbi.nlm.nih.gov/pubmed/34530157
http://dx.doi.org/10.1016/j.mcpro.2021.100148
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author Yang, Yujiao
Zhang, Hong
Guo, Zhenyang
Zou, Siwei
Long, Fei
Wu, Jiacheng
Li, Peng
Zhao, Guo-ping
Zhao, Wei
author_facet Yang, Yujiao
Zhang, Hong
Guo, Zhenyang
Zou, Siwei
Long, Fei
Wu, Jiacheng
Li, Peng
Zhao, Guo-ping
Zhao, Wei
author_sort Yang, Yujiao
collection PubMed
description Lysine acylations are reversible and ubiquitous post-translational modifications that play critical roles in regulating multiple cellular processes. In the current study, highly abundant and dynamic acetylation, besides succinylation, was uncovered in a soil bacterium, Streptomyces coelicolor. By affinity enrichment using anti–acetyl-lysine antibody and the following LC−MS/MS analysis, a total of 1298 acetylation sites among 601 proteins were identified. Bioinformatics analyses suggested that these acetylated proteins have diverse subcellular localization and were enriched in a wide range of biological functions. Specifically, a majority of the acetylated proteins were also succinylated in the tricarboxylic acid cycle and protein translation pathways, and the bimodification occurred at the same sites in some proteins. The acetylation and succinylation sites were quantified by knocking out either the deacetylase ScCobB1 or the desuccinylase ScCobB2, demonstrating a possible competitive relationship between the two acylations. Moreover, in vitro experiments using synthetically modified peptides confirmed the regulatory crosstalk between the two sirtuins, which may be involved in the collaborative regulation of cell physiology. Collectively, these results provided global insights into the S. coelicolor acylomes and laid a foundation for characterizing the regulatory roles of the crosstalk between lysine acetylation and succinylation in the future.
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spelling pubmed-84980042021-10-12 Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways Yang, Yujiao Zhang, Hong Guo, Zhenyang Zou, Siwei Long, Fei Wu, Jiacheng Li, Peng Zhao, Guo-ping Zhao, Wei Mol Cell Proteomics Research Lysine acylations are reversible and ubiquitous post-translational modifications that play critical roles in regulating multiple cellular processes. In the current study, highly abundant and dynamic acetylation, besides succinylation, was uncovered in a soil bacterium, Streptomyces coelicolor. By affinity enrichment using anti–acetyl-lysine antibody and the following LC−MS/MS analysis, a total of 1298 acetylation sites among 601 proteins were identified. Bioinformatics analyses suggested that these acetylated proteins have diverse subcellular localization and were enriched in a wide range of biological functions. Specifically, a majority of the acetylated proteins were also succinylated in the tricarboxylic acid cycle and protein translation pathways, and the bimodification occurred at the same sites in some proteins. The acetylation and succinylation sites were quantified by knocking out either the deacetylase ScCobB1 or the desuccinylase ScCobB2, demonstrating a possible competitive relationship between the two acylations. Moreover, in vitro experiments using synthetically modified peptides confirmed the regulatory crosstalk between the two sirtuins, which may be involved in the collaborative regulation of cell physiology. Collectively, these results provided global insights into the S. coelicolor acylomes and laid a foundation for characterizing the regulatory roles of the crosstalk between lysine acetylation and succinylation in the future. American Society for Biochemistry and Molecular Biology 2021-09-14 /pmc/articles/PMC8498004/ /pubmed/34530157 http://dx.doi.org/10.1016/j.mcpro.2021.100148 Text en © 2021 The Authors https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research
Yang, Yujiao
Zhang, Hong
Guo, Zhenyang
Zou, Siwei
Long, Fei
Wu, Jiacheng
Li, Peng
Zhao, Guo-ping
Zhao, Wei
Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways
title Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways
title_full Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways
title_fullStr Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways
title_full_unstemmed Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways
title_short Global Insights Into Lysine Acylomes Reveal Crosstalk Between Lysine Acetylation and Succinylation in Streptomyces coelicolor Metabolic Pathways
title_sort global insights into lysine acylomes reveal crosstalk between lysine acetylation and succinylation in streptomyces coelicolor metabolic pathways
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8498004/
https://www.ncbi.nlm.nih.gov/pubmed/34530157
http://dx.doi.org/10.1016/j.mcpro.2021.100148
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