Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus

Abstract Lysine acetylation is a major post-translational modification that plays important regulatory roles in diverse biological processes to perform various cellular functions in both eukaryotes and prokaryotes. However, roles of lysine acetylation in plant fungal pathogens were less studied. Her...

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Autores principales:	Xiaomei Sun, Zhigang Li, Hang Liu, Jun Yang, Wenxing Liang, You-Liang Peng, Jinguang Huang
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/a5de3931a2204bbdb335c89ba070ee99
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spelling	oai:doaj.org-article:a5de3931a2204bbdb335c89ba070ee992021-12-02T15:06:18ZLarge-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus10.1038/s41598-017-15655-42045-2322https://doaj.org/article/a5de3931a2204bbdb335c89ba070ee992017-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-15655-4https://doaj.org/toc/2045-2322Abstract Lysine acetylation is a major post-translational modification that plays important regulatory roles in diverse biological processes to perform various cellular functions in both eukaryotes and prokaryotes. However, roles of lysine acetylation in plant fungal pathogens were less studied. Here, we provided the first lysine acetylome of vegetative hyphae of the rice blast fungus Magnaporthe oryzae through a combination of highly sensitive immune-affinity purification and high-resolution LC-MS/MS. This lysine acetylome had 2,720 acetylation sites in 1,269 proteins. The lysine acetylated proteins were involved indiverse cellular functions, and located in 820 nodes and 7,709 edges among the protein-protein interaction network. Several amino acid residues nearby the lysine acetylation sites were conserved, including KacR, KacK, and KacH. Importantly, dozens of lysine acetylated proteins are found to be important to vegetative hyphal growth and fungal pathogenicity. Taken together, our results provided the first comprehensive view of lysine acetylome of M.oryzae and suggested protein lysine acetylation played important roles to fungal development and pathogenicity.Xiaomei SunZhigang LiHang LiuJun YangWenxing LiangYou-Liang PengJinguang HuangNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Xiaomei Sun Zhigang Li Hang Liu Jun Yang Wenxing Liang You-Liang Peng Jinguang Huang Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus
description	Abstract Lysine acetylation is a major post-translational modification that plays important regulatory roles in diverse biological processes to perform various cellular functions in both eukaryotes and prokaryotes. However, roles of lysine acetylation in plant fungal pathogens were less studied. Here, we provided the first lysine acetylome of vegetative hyphae of the rice blast fungus Magnaporthe oryzae through a combination of highly sensitive immune-affinity purification and high-resolution LC-MS/MS. This lysine acetylome had 2,720 acetylation sites in 1,269 proteins. The lysine acetylated proteins were involved indiverse cellular functions, and located in 820 nodes and 7,709 edges among the protein-protein interaction network. Several amino acid residues nearby the lysine acetylation sites were conserved, including KacR, KacK, and KacH. Importantly, dozens of lysine acetylated proteins are found to be important to vegetative hyphal growth and fungal pathogenicity. Taken together, our results provided the first comprehensive view of lysine acetylome of M.oryzae and suggested protein lysine acetylation played important roles to fungal development and pathogenicity.
format	article
author	Xiaomei Sun Zhigang Li Hang Liu Jun Yang Wenxing Liang You-Liang Peng Jinguang Huang
author_facet	Xiaomei Sun Zhigang Li Hang Liu Jun Yang Wenxing Liang You-Liang Peng Jinguang Huang
author_sort	Xiaomei Sun
title	Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus
title_short	Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus
title_full	Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus
title_fullStr	Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus
title_full_unstemmed	Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus
title_sort	large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/a5de3931a2204bbdb335c89ba070ee99
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Large-scale identification of lysine acetylated proteins in vegetative hyphae of the rice blast fungus

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