Proteomics

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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): LTQ Orbitrap Elite

ORGANISM(S): Halobacterium Salinarum

TISSUE(S): Cell Culture

SUBMITTER: Jingfang Liu  

LAB HEAD: Hua Xiang

PROVIDER: PXD006211 | Pride | 2017-08-07

REPOSITORIES: Pride

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

Liu Jingfang J   Wang Qian Q   Jiang Xiongjian X   Yang Haibo H   Zhao Dahe D   Han Jing J   Luo Yuanming Y   Xiang Hua H  

Journal of proteome research 20170822 9

Lysine acetylation is a reversible and highly regulated post-translational modification that plays a critical role in regulating many aspects of cellular processes, both in bacteria and in eukaryotes. However, this modification has not been systematically studied in archaea. Herein, we report the lysine acetylome of a model haloarchaeon, Haloferax mediterranei. Using immunoaffinity enrichment and LC-MS/MS analysis, we identified 1017 acetylation sites in 643 proteins, accounting for 17.3% of the  ...[more]

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