Proteomics

Dataset Information

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Lysine acylation in Bacillus subtilis


ABSTRACT: We identified 2,536 lysine acetylated sites, 4,723 propionylated sites, 2,150 succinylated sites and 3,001 malonylated sites in Bacillus subtilis

ORGANISM(S): Bacillus Subtilis Subsp. Subtilis Str. 168

SUBMITTER: Minjia Tan  

PROVIDER: PXD038448 | iProX | Mon Nov 28 00:00:00 GMT 2022

REPOSITORIES: iProX

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Publications

Global landscape of lysine acylomes in Bacillus subtilis.

Zhang Mingya M   Liu TianXian T   Wang Le L   Huang Yuqi Y   Fan Rufeng R   Ma Ke K   Kan Yunbo Y   Tan Minjia M   Xu Jun-Yu JY  

Journal of proteomics 20221103


Lysine acetylation is a common posttranslational modification that regulates numerous biochemical functions in both eukaryotic and prokaryotic species. In addition, several new non-acetyl acylations are structurally different from lysine acetylation and participate in diverse physiological functions. Here, a comprehensive analysis of several lysine acylomes was performed by combining the high-affinity antibody enrichment with high-resolution LC-MS/MS. In total, we identified 2536 lysine acetylat  ...[more]

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