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, inclu

SUBMITTER: Lv B 

PROVIDER: S-EPMC4933888 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature