Chapter title |
Identification of Acetylated Proteins in Borrelia burgdorferi
|
---|---|
Chapter number | 14 |
Book title |
Borrelia burgdorferi
|
Published in |
Methods in molecular biology, January 2018
|
DOI | 10.1007/978-1-4939-7383-5_14 |
Pubmed ID | |
Book ISBNs |
978-1-4939-7382-8, 978-1-4939-7383-5
|
Authors |
Youyun Yang, Alan Wolfe, X. Frank Yang |
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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