Cargando…

Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum

Fusarium oxysporum is one of the most abundant and diverse fungal species found in soils and includes nonpathogenic, endophytic, and pathogenic strains affecting a broad range of plant and animal hosts. Conidiation is the major mode of reproduction in many filamentous fungi, but the regulation of th...

Descripción completa

Detalles Bibliográficos
Autores principales: Lv, Fangjiao, Xu, Yang, Gabriel, Dean W., Wang, Xue, Zhang, Ning, Liang, Wenxing
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9134102/
https://www.ncbi.nlm.nih.gov/pubmed/35398590
http://dx.doi.org/10.1016/j.mcpro.2022.100231
_version_ 1784713718370664448
author Lv, Fangjiao
Xu, Yang
Gabriel, Dean W.
Wang, Xue
Zhang, Ning
Liang, Wenxing
author_facet Lv, Fangjiao
Xu, Yang
Gabriel, Dean W.
Wang, Xue
Zhang, Ning
Liang, Wenxing
author_sort Lv, Fangjiao
collection PubMed
description Fusarium oxysporum is one of the most abundant and diverse fungal species found in soils and includes nonpathogenic, endophytic, and pathogenic strains affecting a broad range of plant and animal hosts. Conidiation is the major mode of reproduction in many filamentous fungi, but the regulation of this process is largely unknown. Lysine acetylation (Kac) is an evolutionarily conserved and widespread posttranslational modification implicated in regulation of multiple metabolic processes. A total of 62 upregulated and 49 downregulated Kac proteins were identified in sporulating mycelia versus nonsporulating mycelia of F. oxysporum. Diverse cellular proteins, including glycolytic enzymes, ribosomal proteins, and endoplasmic reticulum–resident molecular chaperones, were differentially acetylated in the sporulation process. Altered Kac levels of three endoplasmic reticulum–resident molecular chaperones, PDI(K70), HSP70(K604), and HSP40(K32) were identified that with important roles in F. oxysporum conidiation. Specifically, K70 acetylation (K70ac) was found to be crucial for maintaining stability and activity of protein disulphide isomerase and the K604ac of HSP70 and K32ac of HSP40 suppressed the detoxification ability of these heat shock proteins, resulting in higher levels of protein aggregation. During conidial formation, an increased level of PDI(K70ac) and decreased levels of HSP70(K604ac) and HSP40(K32ac) contributed to the proper processing of unfolded proteins and eliminated protein aggregation, which is beneficial for dramatic cell biological remodeling during conidiation in F. oxysporum.
format Online
Article
Text
id pubmed-9134102
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher American Society for Biochemistry and Molecular Biology
record_format MEDLINE/PubMed
spelling pubmed-91341022022-06-04 Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum Lv, Fangjiao Xu, Yang Gabriel, Dean W. Wang, Xue Zhang, Ning Liang, Wenxing Mol Cell Proteomics Research Fusarium oxysporum is one of the most abundant and diverse fungal species found in soils and includes nonpathogenic, endophytic, and pathogenic strains affecting a broad range of plant and animal hosts. Conidiation is the major mode of reproduction in many filamentous fungi, but the regulation of this process is largely unknown. Lysine acetylation (Kac) is an evolutionarily conserved and widespread posttranslational modification implicated in regulation of multiple metabolic processes. A total of 62 upregulated and 49 downregulated Kac proteins were identified in sporulating mycelia versus nonsporulating mycelia of F. oxysporum. Diverse cellular proteins, including glycolytic enzymes, ribosomal proteins, and endoplasmic reticulum–resident molecular chaperones, were differentially acetylated in the sporulation process. Altered Kac levels of three endoplasmic reticulum–resident molecular chaperones, PDI(K70), HSP70(K604), and HSP40(K32) were identified that with important roles in F. oxysporum conidiation. Specifically, K70 acetylation (K70ac) was found to be crucial for maintaining stability and activity of protein disulphide isomerase and the K604ac of HSP70 and K32ac of HSP40 suppressed the detoxification ability of these heat shock proteins, resulting in higher levels of protein aggregation. During conidial formation, an increased level of PDI(K70ac) and decreased levels of HSP70(K604ac) and HSP40(K32ac) contributed to the proper processing of unfolded proteins and eliminated protein aggregation, which is beneficial for dramatic cell biological remodeling during conidiation in F. oxysporum. American Society for Biochemistry and Molecular Biology 2022-04-08 /pmc/articles/PMC9134102/ /pubmed/35398590 http://dx.doi.org/10.1016/j.mcpro.2022.100231 Text en © 2022 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
Lv, Fangjiao
Xu, Yang
Gabriel, Dean W.
Wang, Xue
Zhang, Ning
Liang, Wenxing
Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum
title Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum
title_full Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum
title_fullStr Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum
title_full_unstemmed Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum
title_short Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum
title_sort quantitative proteomic analysis reveals important roles of the acetylation of er-resident molecular chaperones for conidiation in fusarium oxysporum
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9134102/
https://www.ncbi.nlm.nih.gov/pubmed/35398590
http://dx.doi.org/10.1016/j.mcpro.2022.100231
work_keys_str_mv AT lvfangjiao quantitativeproteomicanalysisrevealsimportantrolesoftheacetylationoferresidentmolecularchaperonesforconidiationinfusariumoxysporum
AT xuyang quantitativeproteomicanalysisrevealsimportantrolesoftheacetylationoferresidentmolecularchaperonesforconidiationinfusariumoxysporum
AT gabrieldeanw quantitativeproteomicanalysisrevealsimportantrolesoftheacetylationoferresidentmolecularchaperonesforconidiationinfusariumoxysporum
AT wangxue quantitativeproteomicanalysisrevealsimportantrolesoftheacetylationoferresidentmolecularchaperonesforconidiationinfusariumoxysporum
AT zhangning quantitativeproteomicanalysisrevealsimportantrolesoftheacetylationoferresidentmolecularchaperonesforconidiationinfusariumoxysporum
AT liangwenxing quantitativeproteomicanalysisrevealsimportantrolesoftheacetylationoferresidentmolecularchaperonesforconidiationinfusariumoxysporum