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Systematic Analysis of Lysine Acetylation in the Halophilic Archaeon <i>Haloferax mediterranei</i>
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, <i>Haloferax mediterranei.</i> Using immunoaffinity enrichment
and 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
mainly distributes in cytoplasm (94%) and participates in protein
biosynthesis and carbon metabolism. Specifically, the acetylation
of key enzymes in PHBV biosynthesis further suggested that acetylation
plays a key role in the energy and carbon storage. In addition, a
survey of the acetylome revealed a universal rule in acetylated motifs:
a positively charged residue (K, R, or H) located downstream of acetylated
lysine at the positions +1, +2, or +3. Interestingly, we identified
acetylation in several replication initiation proteins Cdc6; mutation
on the acetylated site of Cdc6A destroyed the Autonomous Replication
Sequence (ARS) activity of its adjacent origin <i>oriC1</i>. Our study indicates that lysine acetylation is an abundant modification
in <i>H. mediterranei</i>, and plays key roles in the
processes of replication, protein biosynthesis, central metabolism,
and carbon storage. This acetylome of <i>H. mediterranei</i> provides opportunities to explore the physiological role of acetylation
in halophilic archaea