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Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis

BACKGROUND: Lysine 2-hydroxyisobutyrylation (Khib) is a novel and conserved post-translational modification (PTM). Frankliniella occidentalis are economically important agricultural pests globally and also notorious for vectoring destructive plant viruses. To better study the disease transmission me...

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Autores principales: Ding, Chengying, Song, Liyun, Li, Ying, Shen, Lili, Liu, Dongyang, Wang, Fenglong, Lin, Zhonglong, Yang, Jinguang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9422105/
https://www.ncbi.nlm.nih.gov/pubmed/36038823
http://dx.doi.org/10.1186/s12864-022-08841-w
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author Ding, Chengying
Song, Liyun
Li, Ying
Shen, Lili
Liu, Dongyang
Wang, Fenglong
Lin, Zhonglong
Yang, Jinguang
author_facet Ding, Chengying
Song, Liyun
Li, Ying
Shen, Lili
Liu, Dongyang
Wang, Fenglong
Lin, Zhonglong
Yang, Jinguang
author_sort Ding, Chengying
collection PubMed
description BACKGROUND: Lysine 2-hydroxyisobutyrylation (Khib) is a novel and conserved post-translational modification (PTM). Frankliniella occidentalis are economically important agricultural pests globally and also notorious for vectoring destructive plant viruses. To better study the disease transmission mechanism of F. occidentalis, it is necessary to conduct in-depth analysis of it. So far, no Khib modification of insects has been reported. RESULTS: In this study, a proteome-wide analysis of Khib modifications in F. occidentalis was analyzed for the first time through the combination of high performance liquid chromatography fractionation technology and 2-hydroxyisobutyrylated peptide enrichment and other advanced technologies, 4093 Khib sites were identified on 1125 modified proteins. Bioinformatics and functional enrichment analyses showed that Khib-modified proteins were significantly enriched in many cell compartments and pathways, especially related to various cellular components and biological processes, and were more concentrated in ribosomes and proteasome subunits, involved in energy metabolism, protein synthesis and degradation, compared to the other nine species including Japonica rice, Homo sapiens, P. patens, Botrytis, Ustilaginoidea virens, Saccharomyces cerevisiae, T. gondii, C. albicans, and F. oxysporum. And Khib sites on virus-interacting insect proteins were discovered for the first time, such as cyclophilin and endoCP-GN. CONCLUSIONS: After three repeated experiments, we found a total of 4093 Khib sites on 1125 proteins. These modified proteins are mainly concentrated in ribosomes and proteasome subunits, and are widely involved in a variety of critical biological activities and metabolic processes of F. occidentalis. In addition, for the first time, Khib modification sites are found on the proteome of F. occidentalis, and these sites could be acted as for the virus interaction, including cyclophilin and endoCP-GN. The global map of 2-hydroxyisobutyrylation in thrips is an invaluable resource to better understand the biological processes of thrips and provide new means for disease control and mitigation of pest damage to crops. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12864-022-08841-w.
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spelling pubmed-94221052022-08-30 Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis Ding, Chengying Song, Liyun Li, Ying Shen, Lili Liu, Dongyang Wang, Fenglong Lin, Zhonglong Yang, Jinguang BMC Genomics Research BACKGROUND: Lysine 2-hydroxyisobutyrylation (Khib) is a novel and conserved post-translational modification (PTM). Frankliniella occidentalis are economically important agricultural pests globally and also notorious for vectoring destructive plant viruses. To better study the disease transmission mechanism of F. occidentalis, it is necessary to conduct in-depth analysis of it. So far, no Khib modification of insects has been reported. RESULTS: In this study, a proteome-wide analysis of Khib modifications in F. occidentalis was analyzed for the first time through the combination of high performance liquid chromatography fractionation technology and 2-hydroxyisobutyrylated peptide enrichment and other advanced technologies, 4093 Khib sites were identified on 1125 modified proteins. Bioinformatics and functional enrichment analyses showed that Khib-modified proteins were significantly enriched in many cell compartments and pathways, especially related to various cellular components and biological processes, and were more concentrated in ribosomes and proteasome subunits, involved in energy metabolism, protein synthesis and degradation, compared to the other nine species including Japonica rice, Homo sapiens, P. patens, Botrytis, Ustilaginoidea virens, Saccharomyces cerevisiae, T. gondii, C. albicans, and F. oxysporum. And Khib sites on virus-interacting insect proteins were discovered for the first time, such as cyclophilin and endoCP-GN. CONCLUSIONS: After three repeated experiments, we found a total of 4093 Khib sites on 1125 proteins. These modified proteins are mainly concentrated in ribosomes and proteasome subunits, and are widely involved in a variety of critical biological activities and metabolic processes of F. occidentalis. In addition, for the first time, Khib modification sites are found on the proteome of F. occidentalis, and these sites could be acted as for the virus interaction, including cyclophilin and endoCP-GN. The global map of 2-hydroxyisobutyrylation in thrips is an invaluable resource to better understand the biological processes of thrips and provide new means for disease control and mitigation of pest damage to crops. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s12864-022-08841-w. BioMed Central 2022-08-29 /pmc/articles/PMC9422105/ /pubmed/36038823 http://dx.doi.org/10.1186/s12864-022-08841-w Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
spellingShingle Research
Ding, Chengying
Song, Liyun
Li, Ying
Shen, Lili
Liu, Dongyang
Wang, Fenglong
Lin, Zhonglong
Yang, Jinguang
Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis
title Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis
title_full Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis
title_fullStr Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis
title_full_unstemmed Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis
title_short Proteome-wide analysis of lysine 2-hydroxyisobutyrylation in Frankliniella occidentalis
title_sort proteome-wide analysis of lysine 2-hydroxyisobutyrylation in frankliniella occidentalis
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9422105/
https://www.ncbi.nlm.nih.gov/pubmed/36038823
http://dx.doi.org/10.1186/s12864-022-08841-w
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