Identification of Acetylated Proteins in Borrelia burgdorferi Journal Article

Local Library Link: Find It @ Loyola

Authors: Yang, Y; Wolfe, A.; Yang, X. F.
Article Title: Identification of Acetylated Proteins in Borrelia burgdorferi
Abstract: Posttranslational modification (PTM) of proteins has emerged as a major regulatory mechanism in all three domains of life. One emerging PTM is Nepsilon-lysine acetylation-the acetylation of the epsilon amino group of lysine residues. Nepsilon-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 Nepsilon-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 Nepsilon-lysine acetylated proteins in B. burgdorferi.
Journal Title: Methods in Molecular Biology
Volume: 1690
ISSN: 1940-6029
Publisher: Unknown  
Journal Place: United States
Date Published: 2018
Start Page: 177
End Page: 182
Language: eng
DOI/URL:

10.1007/978-1-4939-7383-5_14
Notes: LR: 20180325; GR: R01 AI083640/AI/NIAID NIH HHS/United States; JID: 9214969; NIHMS948626; OTO: NOTNLM; 2017/10/17 06:00 [entrez]; 2017/10/17 06:00 [pubmed]; 2017/10/17 06:00 [medline]; ppublish