Abstract

The past decade highlighted Nε-lysine acetylation as a prevalent posttranslational modification in bacteria. However, knowledge regarding the physiological importance and temporal regulation of acetylation has remained limited. To uncover potential regulatory roles for acetylation, we analyzed how acetylation patterns and abundances change between growth phases in B. subtilis. To demonstrate that the identification of cell growth-dependent modifications can point to critical regulatory acetylation events, we further characterized MreB, the cell shape-determining protein. Our findings led us to propose a role for MreB acetylation in controlling cell width by restricting cell wall growth.

Highlights

  • The physiological importance of N␧-lysine acetylation as a regulatory posttranslational modification (PTM) is emphasized by the association of its dysregulation with heart disease and aging [1], obesity and diabetes [2], Alzheimer’s disease [3], and certain cancers [4]

  • Lysine acetylation is prevalent in B. subtilis and temporally regulated throughout growth

  • We chose to characterize the dynamic changes occurring during logarithmic- and stationary-phase growth, because differential acetylation of lysine residues might occur during rapid growth and be of particular relevance for cells progressing from the log into the stat phase

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Summary

Introduction

The physiological importance of N␧-lysine acetylation as a regulatory posttranslational modification (PTM) is emphasized by the association of its dysregulation with heart disease and aging [1], obesity and diabetes [2], Alzheimer’s disease [3], and certain cancers [4]. The activity of AcsA is finely tuned to the levels of acetyl-CoA and NADϩ This mechanism is evolutionarily conserved, even in human mitochondria [31, 44,45,46,47,48,49,50]. Based on our differential acetylome analysis, we conducted a functional analysis of the essential cell shapedetermining protein MreB, which exhibited a stationary-phase-specific increase in acetylation at a single lysine residue. This characterization suggested a contribution of MreB acetylation in regulating cell wall growth

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