Abstract
Posttranslational modification (PTM) of proteins has emerged as a major regulatory mechanism in all three domains of life. One emerging PTM is Nε-lysine acetylation—the acetylation of the epsilon amino group of lysine residues. Nε-lysine acetylation is known to regulate multiple cellular processes. In eukaryotes, it regulates chromatin structure, transcription, metabolism, signal transduction, and the cytoskeleton. Recently, multiple groups have detected Nε-lysine acetylation in diverse bacterial phyla, but no work on protein acetylation in Borrelia burgdorferi has been reported. Here, we describe a step-by-step protocol to identify Nε-lysine acetylated proteins in B. burgdorferi.
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Acknowledgments
This work was supported by grants from the HHS | NIH | National Institute of Allergy and Infectious Diseases (NIAID) (AI4684064 to XFY).
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Yang, Y., Wolfe, A., Yang, X.F. (2018). Identification of Acetylated Proteins in Borrelia burgdorferi . In: Pal, U., Buyuktanir, O. (eds) Borrelia burgdorferi. Methods in Molecular Biology, vol 1690. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7383-5_14
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DOI: https://doi.org/10.1007/978-1-4939-7383-5_14
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