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Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern

Abstract : An organism’s entire protein modification repertoire has yet to be comprehensively mapped. N-myristoylation (MYR) is a crucial eukaryotic N-terminal protein modification. Here we mapped complete Homo sapiens and Arabidopsis thaliana myristoylomes. The crystal structures of human modifier NMT1 complexed with reactive and nonreactive target-mimicking peptide ligands revealed unexpected binding clefts and a modifier recognition pattern. This information allowed integrated mapping of myristoylomes using peptide macroarrays, dedicated prediction algorithms, and in vivo mass spectrometry. Global MYR profiling at the genomic scale identified over a thousand novel, heterogeneous targets in both organisms. Surprisingly, MYR involved a non-negligible set of overlapping targets with N-acetylation, and the sequence signature marks for a third proximal acylation—S-palmitoylation—were genomically imprinted, allowing recognition of sequences exhibiting both acylations. Together, the data extend the N-end rule concept for Gly-starting proteins to subcellular compartmentalization and reveal the main neighbors influencing protein modification profiles and consequent cell fate.
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https://hal-cea.archives-ouvertes.fr/cea-01873857
Contributor : Bruno Savelli <>
Submitted on : Thursday, September 13, 2018 - 4:15:44 PM
Last modification on : Friday, September 11, 2020 - 3:17:59 AM

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Benoît Castrec, Cyril Dian, Sarah Ciccone, Coralie Ebert, Willy Bienvenut, et al.. Structural and genomic decoding of human and plant myristoylomes reveals a definitive recognition pattern. Nature Chemical Biology, Nature Publishing Group, 2018, 14, pp.671 - 679. ⟨10.1038/s41589-018-0077-5⟩. ⟨cea-01873857⟩

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