Systematic Analysis of Lysine Acetylation in the Halophilic Archaeon Haloferax mediterranei
2017
Lysine
acetylationis 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
lysineacetylome of a model haloarchaeon,
Haloferax mediterranei. Using immunoaffinity enrichment and LC–MS/MS analysis, we identified 1017
acetylationsites in 643 proteins, accounting for 17.3% of the total proteins in this haloarchaeon. Bioinformatics analysis indicated that
lysine
acetylationmainly distributes in cytoplasm (94%) and participates in
protein biosynthesisand carbon metabolism. Specifically, the
acetylationof key enzymes in PHBV biosynthesis further suggested that
acetylationplays a key role in the energy and carbon storage. In addition, a survey of the acetylome revealed a universal rule in
acetylatedmotifs: a positively charged residue (K, R, or H) located downstream of
acetylated
lysinea...
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