Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>

ABSTRACT Candida albicans is the most common human fungal pathogen, causing diseases ranging from mucosal to systemic infections for both immunocompetent and immunocompromised individuals. Lysine 2-hydroxyisobutyrylation is a highly conserved posttranslational modification found in a wide variety of...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Hailin Zheng, Nana Song, Xiaowei Zhou, Huan Mei, Dongmei Li, Xiaofang Li, Weida Liu
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2021
Materias:	posttranslational modification lysine 2-hydroxyisobutyrylation proteome Candida albicans Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/14058db5597c40a09e7dba15b45cfef6
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:14058db5597c40a09e7dba15b45cfef6
record_format	dspace
spelling	oai:doaj.org-article:14058db5597c40a09e7dba15b45cfef62021-12-02T17:07:26ZProteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>10.1128/mSystems.01129-202379-5077https://doaj.org/article/14058db5597c40a09e7dba15b45cfef62021-02-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSystems.01129-20https://doaj.org/toc/2379-5077ABSTRACT Candida albicans is the most common human fungal pathogen, causing diseases ranging from mucosal to systemic infections for both immunocompetent and immunocompromised individuals. Lysine 2-hydroxyisobutyrylation is a highly conserved posttranslational modification found in a wide variety of organisms. In this study, we surveyed the biological impact of 2-hydroxyisobutyrylation on lysine residuals (Khib) in C. albicans. Using an antibody enrichment approach along with the traditional liquid chromatography-tandem mass spectrometry (LC-MS/MS) method, we analyzed the pattern of Khib-modified proteins and sites in one wild-type strain of C. albicans. We identified 1,438 Khib-modified proteins with 6,659 modified sites in this strain, and a more detailed bioinformatics analysis indicated that the Khib-modified proteins are involved in a wide range of cellular functions with diverse subcellular locations. Functional enrichment analysis featured several prominent functional pathways, including ribosome, biosynthesis of antibiotics, biosynthesis of secondary metabolites, biosynthesis of amino acids and carbon metabolism, of which the ribosome pathway is the most affected pathway. Even compared with the reported numbers of lysine acetylation (Kac) and succinylation (Ksuc) sites, the numbers of Khib-modified sites on ribosomal proteins remained the highest for C. albicans. These bioinformatic results suggest that 2-hydroxyisobutyrylation may play an indispensable role in the regulation of the ribosomal biogenesis and protein translation. Findings in this study may provide new insights for studying posttranslational modification (PTM)-associated mechanisms in fungal development and pathogenicity. IMPORTANCE C. albicans is one of the most commonly reported fungal pathogens in mucosal and systemic infections. A better understanding of its growth habits and metabolic processes in the host should help improve defense strategies. The newly discovered protein posttranslational modification (PTM) on histones is one epigenetic mechanism which has been linked to many pathogenic events, including cancers. The types of PTM and their pathogenic roles in C. albicans are still somewhat poorly understood, even though studies of C. albicans based on acetylation inhibitors have shed some light on their function, and it seems that PTMs regulate pathogenic adhesion factors. Here, we quantified and analyzed the occurrence of lysine 2-hydroxyisobutyrylation (Khib) in C. albicans. The Khib-modified proteins are enriched with respect to carbon metabolism, ribosomal biogenesis, and protein translation in C. albicans.Hailin ZhengNana SongXiaowei ZhouHuan MeiDongmei LiXiaofang LiWeida LiuAmerican Society for Microbiologyarticleposttranslational modificationlysine 2-hydroxyisobutyrylationproteomeCandida albicansposttranslational modificationMicrobiologyQR1-502ENmSystems, Vol 6, Iss 1 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	posttranslational modification lysine 2-hydroxyisobutyrylation proteome Candida albicans posttranslational modification Microbiology QR1-502
spellingShingle	posttranslational modification lysine 2-hydroxyisobutyrylation proteome Candida albicans posttranslational modification Microbiology QR1-502 Hailin Zheng Nana Song Xiaowei Zhou Huan Mei Dongmei Li Xiaofang Li Weida Liu Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>
description	ABSTRACT Candida albicans is the most common human fungal pathogen, causing diseases ranging from mucosal to systemic infections for both immunocompetent and immunocompromised individuals. Lysine 2-hydroxyisobutyrylation is a highly conserved posttranslational modification found in a wide variety of organisms. In this study, we surveyed the biological impact of 2-hydroxyisobutyrylation on lysine residuals (Khib) in C. albicans. Using an antibody enrichment approach along with the traditional liquid chromatography-tandem mass spectrometry (LC-MS/MS) method, we analyzed the pattern of Khib-modified proteins and sites in one wild-type strain of C. albicans. We identified 1,438 Khib-modified proteins with 6,659 modified sites in this strain, and a more detailed bioinformatics analysis indicated that the Khib-modified proteins are involved in a wide range of cellular functions with diverse subcellular locations. Functional enrichment analysis featured several prominent functional pathways, including ribosome, biosynthesis of antibiotics, biosynthesis of secondary metabolites, biosynthesis of amino acids and carbon metabolism, of which the ribosome pathway is the most affected pathway. Even compared with the reported numbers of lysine acetylation (Kac) and succinylation (Ksuc) sites, the numbers of Khib-modified sites on ribosomal proteins remained the highest for C. albicans. These bioinformatic results suggest that 2-hydroxyisobutyrylation may play an indispensable role in the regulation of the ribosomal biogenesis and protein translation. Findings in this study may provide new insights for studying posttranslational modification (PTM)-associated mechanisms in fungal development and pathogenicity. IMPORTANCE C. albicans is one of the most commonly reported fungal pathogens in mucosal and systemic infections. A better understanding of its growth habits and metabolic processes in the host should help improve defense strategies. The newly discovered protein posttranslational modification (PTM) on histones is one epigenetic mechanism which has been linked to many pathogenic events, including cancers. The types of PTM and their pathogenic roles in C. albicans are still somewhat poorly understood, even though studies of C. albicans based on acetylation inhibitors have shed some light on their function, and it seems that PTMs regulate pathogenic adhesion factors. Here, we quantified and analyzed the occurrence of lysine 2-hydroxyisobutyrylation (Khib) in C. albicans. The Khib-modified proteins are enriched with respect to carbon metabolism, ribosomal biogenesis, and protein translation in C. albicans.
format	article
author	Hailin Zheng Nana Song Xiaowei Zhou Huan Mei Dongmei Li Xiaofang Li Weida Liu
author_facet	Hailin Zheng Nana Song Xiaowei Zhou Huan Mei Dongmei Li Xiaofang Li Weida Liu
author_sort	Hailin Zheng
title	Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>
title_short	Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>
title_full	Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>
title_fullStr	Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>
title_full_unstemmed	Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>
title_sort	proteome-wide analysis of lysine 2-hydroxyisobutyrylation in <named-content content-type="genus-species">candida albicans</named-content>
publisher	American Society for Microbiology
publishDate	2021
url	https://doaj.org/article/14058db5597c40a09e7dba15b45cfef6
work_keys_str_mv	AT hailinzheng proteomewideanalysisoflysine2hydroxyisobutyrylationinnamedcontentcontenttypegenusspeciescandidaalbicansnamedcontent AT nanasong proteomewideanalysisoflysine2hydroxyisobutyrylationinnamedcontentcontenttypegenusspeciescandidaalbicansnamedcontent AT xiaoweizhou proteomewideanalysisoflysine2hydroxyisobutyrylationinnamedcontentcontenttypegenusspeciescandidaalbicansnamedcontent AT huanmei proteomewideanalysisoflysine2hydroxyisobutyrylationinnamedcontentcontenttypegenusspeciescandidaalbicansnamedcontent AT dongmeili proteomewideanalysisoflysine2hydroxyisobutyrylationinnamedcontentcontenttypegenusspeciescandidaalbicansnamedcontent AT xiaofangli proteomewideanalysisoflysine2hydroxyisobutyrylationinnamedcontentcontenttypegenusspeciescandidaalbicansnamedcontent AT weidaliu proteomewideanalysisoflysine2hydroxyisobutyrylationinnamedcontentcontenttypegenusspeciescandidaalbicansnamedcontent
_version_	1718381539828432896

Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in <named-content content-type="genus-species">Candida albicans</named-content>

Ejemplares similares