Biochemical and structural analysis of N-myristoyltransferase mediated protein tagging - Archive ouverte HAL
Article Dans Une Revue Methods in Enzymology Année : 2023

Biochemical and structural analysis of N-myristoyltransferase mediated protein tagging

Résumé

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.
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Dates et versions

hal-04234963 , version 1 (10-10-2023)

Identifiants

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Paul Monassa, Frédéric Rivière, Cyril Dian, Frédéric Frottin, Carmela Giglione, et al.. Biochemical and structural analysis of N-myristoyltransferase mediated protein tagging. Methods in Enzymology, 2023, Modifications and Targeting of Protein Termini: Part A, 684, pp.135-166. ⟨10.1016/bs.mie.2023.02.016⟩. ⟨hal-04234963⟩
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