title: Proteome-wide analysis of lysine acetylation in the plant pathogen Botrytis cinerea.
abstract: Lysine acetylation is a dynamic and reversible post-translational modification that plays an important role in diverse cellular processes. Botrytis cinerea is the most thoroughly studied necrotrophic species due to its broad host range and huge economic impact. However, to date, little is known about the functions of lysine acetylation in this plant pathogen. In this study, we determined the lysine acetylome of B. cinerea through the combination of affinity enrichment and high-resolution LC-MS/MS analysis. Overall, 1582 lysine acetylation sites in 954 proteins were identified. Bioinformatics analysis shows that the acetylated proteins are involved in diverse biological functions and show multiple cellular localizations. Several particular amino acids preferred near acetylation sites, including K(ac)Y, K(ac)H, K(ac)***R, K(ac)F, FK(ac) and K(ac)***K, were identified in this organism. Protein interaction network analysis demonstrates that a variety of interactions are modulated by protein acetylation. Interestingly, 6 proteins involved in virulence of B. cinerea, including 3 key components of the high-osmolarity glycerol pathway, were found to be acetylated, suggesting that lysine acetylation plays regulatory roles in pathogenesis. These data provides the first comprehensive view of the acetylome of B. cinerea and serves as a rich resource for functional analysis of lysine acetylation in this plant pathogen.
authors.affiliation: The Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China.
authors.forename: Binna
authors.initials: B
authors.lastname: Lv
authors.affiliation: The Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China.
authors.forename: Qianqian
authors.initials: Q
authors.lastname: Yang
authors.affiliation: The Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China.
authors.forename: Delong
authors.initials: D
authors.lastname: Li
authors.affiliation: The Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China.
authors.forename: Wenxing
authors.initials: W
authors.lastname: Liang
authors.affiliation: The Key Laboratory of Integrated Crop Pest Management of Shandong Province, College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao 266109, China.
authors.forename: Limin
authors.initials: L
authors.lastname: Song
mesh_terms: D000107:Acetylation; D020171:Botrytis / Q000737:chemistry*; D002853:Chromatography, Liquid; D019295:Computational Biology; D005656:Fungal Proteins / Q000032:analysis*; D008239:Lysine / Q000378:metabolism*; D060066:Protein Interaction Maps; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000032:analysis*; D053719:Tandem Mass Spectrometry
chemical_list: D005656:Fungal Proteins; D020543:Proteome; D008239:Lysine