Recombinant Expression and Purification of N-Acetylated Alpha-Synuclein

Methods Mol Biol. 2019:1948:113-121. doi: 10.1007/978-1-4939-9124-2_10.

Abstract

The majority of proteins in eukaryotic cells are subject to amino-terminal (Nt) acetylation. Recombinant protein expressed using prokaryotic expression systems such as E. coli would not normally be Nt-acetylated as these cells lack the appropriate N-α-terminal acetylation complex. Here we describe a simple protocol that allows the recombinant expression and purification of Nt-acetylated alpha-synuclein (aS) from E. coli.

Keywords: Alpha-synuclein; Amino-terminal acetylation; E. coli; N-α-terminal acetyltransferase; NatB; Recombinant protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Cell Line, Tumor
  • Chromatography, Liquid
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Humans
  • Recombinant Proteins / genetics*
  • Recombinant Proteins / isolation & purification*
  • Recombinant Proteins / metabolism
  • alpha-Synuclein / genetics*
  • alpha-Synuclein / isolation & purification*
  • alpha-Synuclein / metabolism

Substances

  • Recombinant Proteins
  • alpha-Synuclein