Escalante Lab

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Rachel Burckhardt

Graduate Student with dissertator status

Area of Study

Studying the Physiological Effects of Reversible Lysine Acetylation in Bacillus subtilis

Research Description

Reversible lysine acetylation (RLA) is a post-translational modification that is conserved in all three domains of life. This process involves the transfer of an acetyl group, most commonly donated by acetyl-Coenzyme A, to a small molecule or a lysine residue of a protein. Acetylation affects diverse cellular processes, such as transcription, translation, primary and secondary metabolism, energy charge, and CoA homeostasis1.

Bacillus subtilis, a Gram-positive, spore-forming soil bacterium, uses RLA as a mechanism to regulate the acetyl-Coenzyme A synthetase (AcsA) AMP-forming enzyme, which converts acetate to acetyl-CoA2. Such RLA control of AcsA-like enzymes is conserved in prokaryotes and eukaryotes, including humans. The genome of B. subtilis encodes 28 putative acetyltransferases, which only a few have been characterized. Using S. enterica as a heterologous host, work is currently in progress to characterize these other acetyltransferases of B. subtilis.

Furthermore, a paper reporting this bacterium’s acetylome, which describes globally acetylated peptides in a cell under specific growth conditions, suggests that protein acetylation in this bacterium impacts a wide variety of processes3. Highlighting the importance of RLA in B. subtilis, strains with impaired acetylation networks display growth defects. The specific aims of my research seek to provide insights into the biochemistry underpinning acetylation-related phenotypes, thus gaining a broader understanding of the physiological role of RLA in B. subtilis.


1Thao, S. and J.C. Escalante-Semerena, Control of protein function by reversible

N(epsilon)-lysine acetylation in bacteria. Curr. Opin. Microbiol., 2011. 14: p. 200-204.

2Gardner, J.G., et al., Control of Acetyl-Coenzyme A Synthetase (AcsA) Activity by Acetylation/Deacetylation without NAD+ Involvement in Bacillus subtilis. J. Bact., 2006. 188: p. 5460-5468.

3Kim, D., The acetylproteome of Gram-positive model bacterium Bacillus subtilis. Proteomics, 2013. 13: p. 1726-1736

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