Proteomics

Dataset Information

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Acetylome analysis of Botrytis cinerea


ABSTRACT: Lysine acetylation of proteins 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.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Botryotinia Fuckeliana (strain B05.10) (noble Rot Fungus) (botrytis Cinerea)

TISSUE(S): Mycelium

SUBMITTER: qianqian yang  

LAB HEAD: Wenxing Liang

PROVIDER: PXD004031 | Pride | 2017-11-02

REPOSITORIES: Pride

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Publications

Proteome-wide analysis of lysine acetylation in the plant pathogen Botrytis cinerea.

Lv Binna B   Yang Qianqian Q   Li Delong D   Liang Wenxing W   Song Limin L  

Scientific reports 20160706


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/M  ...[more]

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