Cargando…

First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta

Lysine acetylation (Kac) plays a critical role in the regulation of many important cellular processes. However, little is known about Kac in Solenopsis invicta, which is among the 100 most dangerous invasive species in the world. Kac in S. invicta was evaluated for the first time in this study. Alto...

Descripción completa

Detalles Bibliográficos
Autores principales: Ye, Jingwen, Li, Jun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7743978/
https://www.ncbi.nlm.nih.gov/pubmed/33326466
http://dx.doi.org/10.1371/journal.pone.0243787
_version_ 1783624341483683840
author Ye, Jingwen
Li, Jun
author_facet Ye, Jingwen
Li, Jun
author_sort Ye, Jingwen
collection PubMed
description Lysine acetylation (Kac) plays a critical role in the regulation of many important cellular processes. However, little is known about Kac in Solenopsis invicta, which is among the 100 most dangerous invasive species in the world. Kac in S. invicta was evaluated for the first time in this study. Altogether, 2387 Kac sites were tested in 992 proteins. The prediction of subcellular localization indicated that most identified proteins were located in the cytoplasm, mitochondria, and nucleus. Venom allergen Sol i 2, Sol i 3, and Sol i 4 were found to be located in the extracellular. The enriched Kac site motifs included Kac H, Kac Y, Kac G, Kac F, Kac T, and Kac W. H, Y, F, and W frequently occurred at the +1 position, whereas G, Y, and T frequently occurred at the –1 position. In the cellular component, acetylated proteins were enriched in the cytoplasmic part, mitochondrial matrix, and cytosolic ribosome. Furthermore, 25 pathways were detected to have significant enrichment. Interestingly, arginine and proline metabolism, as well as phagosome, which are related to immunity, involved several Kac proteins. Sequence alignment analyses demonstrated that V-type proton ATPase subunit G, tubulin alpha chain, and arginine kinase, the acetylated lysine residues, were evolutionarily conserved among different ant species. In the investigation of the interaction network, diverse interactions were adjusted by Kac. The results indicated that Kac may play an important role in the sensitization, cellular energy metabolism, immune response, nerve signal transduction, and response to biotic and abiotic stress of S. invicta. It may be useful to confirm the functions of Kac target proteins for the design of specific and effective drugs to prevent and control this dangerous invasive species.
format Online
Article
Text
id pubmed-7743978
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-77439782020-12-31 First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta Ye, Jingwen Li, Jun PLoS One Research Article Lysine acetylation (Kac) plays a critical role in the regulation of many important cellular processes. However, little is known about Kac in Solenopsis invicta, which is among the 100 most dangerous invasive species in the world. Kac in S. invicta was evaluated for the first time in this study. Altogether, 2387 Kac sites were tested in 992 proteins. The prediction of subcellular localization indicated that most identified proteins were located in the cytoplasm, mitochondria, and nucleus. Venom allergen Sol i 2, Sol i 3, and Sol i 4 were found to be located in the extracellular. The enriched Kac site motifs included Kac H, Kac Y, Kac G, Kac F, Kac T, and Kac W. H, Y, F, and W frequently occurred at the +1 position, whereas G, Y, and T frequently occurred at the –1 position. In the cellular component, acetylated proteins were enriched in the cytoplasmic part, mitochondrial matrix, and cytosolic ribosome. Furthermore, 25 pathways were detected to have significant enrichment. Interestingly, arginine and proline metabolism, as well as phagosome, which are related to immunity, involved several Kac proteins. Sequence alignment analyses demonstrated that V-type proton ATPase subunit G, tubulin alpha chain, and arginine kinase, the acetylated lysine residues, were evolutionarily conserved among different ant species. In the investigation of the interaction network, diverse interactions were adjusted by Kac. The results indicated that Kac may play an important role in the sensitization, cellular energy metabolism, immune response, nerve signal transduction, and response to biotic and abiotic stress of S. invicta. It may be useful to confirm the functions of Kac target proteins for the design of specific and effective drugs to prevent and control this dangerous invasive species. Public Library of Science 2020-12-16 /pmc/articles/PMC7743978/ /pubmed/33326466 http://dx.doi.org/10.1371/journal.pone.0243787 Text en © 2020 Ye, Li http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Ye, Jingwen
Li, Jun
First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta
title First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta
title_full First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta
title_fullStr First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta
title_full_unstemmed First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta
title_short First proteomic analysis of the role of lysine acetylation in extensive functions in Solenopsis invicta
title_sort first proteomic analysis of the role of lysine acetylation in extensive functions in solenopsis invicta
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7743978/
https://www.ncbi.nlm.nih.gov/pubmed/33326466
http://dx.doi.org/10.1371/journal.pone.0243787
work_keys_str_mv AT yejingwen firstproteomicanalysisoftheroleoflysineacetylationinextensivefunctionsinsolenopsisinvicta
AT lijun firstproteomicanalysisoftheroleoflysineacetylationinextensivefunctionsinsolenopsisinvicta