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Identification of Acetylated Proteins in Borrelia burgdorferi

Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1690)

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.

Key words

Borrelia burgdorferi Posttranslational modification Protein acetylation Immunoprecipitation Acetylated lysine protein 

Notes

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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Copyright information

© Springer Science+Business Media LLC 2018

Authors and Affiliations

  1. 1.Department of Microbiology and ImmunologyIndiana University School of MedicineIndianapolisUSA
  2. 2.Department of Microbiology and ImmunologyLoyola University Chicago, Stritch School of MedicineMaywoodUSA

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