Haloferax mediterranei - Systematic Analysis of Lysine Acetylation in the Halophilic Archaeon Haloferax mediterranei

ABSTRACT: We report the lysine acetylproteome of a model haloarchaeon, Haloferax mediterranei. Using Immunoaffinity enrichment, two-dimensional liquid chromatography (2D-LC) and Nano-LC-MS/MS analysis, we identified 1017 acetylation sites in 643 proteins, accounting for 17.3% of the total proteins in this haloarchaeon. Bioinformatics analysis indicated that lysine acetylation has a widespread subcellular distribution and participates in many biological processes, and protein interaction network analysis showed that lysine acetylation might also regulate a wide range of interactions. The proteins that are involved in translation and carbon metabolism consist of the preferred substrates of lysine acetylation. This dataset indicates that lysine acetylation is an abundant and diverse modification in H.mediterranei, providing opportunities to explore the physiological role of acetylation in this haloarchaeon.

INSTRUMENT(S):

ORGANISM(S): Halobacterium Salinarum

TISSUE(S): Cell Culture

SUBMITTER: Jingfang Liu  

LAB HEAD: Hua Xiang

PROVIDER: PXD006211 | Pride | 2017-08-07

REPOSITORIES: Pride