| Literature DB >> 29032545 |
Youyun Yang1, Alan Wolfe2, X Frank Yang3.
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.Entities:
Keywords: Acetylated lysine protein; Borrelia burgdorferi; Immunoprecipitation; Posttranslational modification; Protein acetylation
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Year: 2018 PMID: 29032545 PMCID: PMC5864457 DOI: 10.1007/978-1-4939-7383-5_14
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745