Identification of acetylated proteins in Borrelia burgdorferi

Youyun Yang, Alan Wolfe, X. Frank Yang

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations


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.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Number of pages6
StatePublished - Jan 1 2018

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Acetylated lysine protein
  • Borrelia burgdorferi
  • Immunoprecipitation
  • Posttranslational modification
  • Protein acetylation

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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  • Cite this

    Yang, Y., Wolfe, A., & Yang, X. F. (2018). Identification of acetylated proteins in Borrelia burgdorferi. In Methods in Molecular Biology (pp. 177-182). (Methods in Molecular Biology; Vol. 1690). Humana Press Inc..