Biochemical and structural analysis of N-myristoyltransferase mediated protein tagging

Methods Enzymol. 2023:684:135-166. doi: 10.1016/bs.mie.2023.02.016. Epub 2023 Mar 28.

Abstract

N-terminal myristoylation is an essential eukaryotic modification crucial for cellular homeostasis in the context of many physiological processes. Myristoylation is a lipid modification resulting in a C14 saturated fatty acid addition. This modification is challenging to capture due to its hydrophobicity, low abundance of target substrates, and the recent discovery of unexpected NMT reactivity including myristoylation of lysine side chains and N-acetylation in addition to classical N-terminal Gly-myristoylation. This chapter details the high-end approaches developed to characterize the different features of N-myristoylation and its targets through in vitro and in vivo labeling.

Keywords: Acetylation; Fatty acid; Glycine; Lysine; Myristoylation; N-myristoyltransferase; N-terminus; Protein acylation; Protein modification.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases* / metabolism
  • Fatty Acids*
  • Lysine
  • Myristic Acid / metabolism

Substances

  • glycylpeptide N-tetradecanoyltransferase
  • Acyltransferases
  • Myristic Acid
  • Fatty Acids
  • Lysine