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

Castrec, Benoit; Dian, Cyril; Ciccone, Sarah; Ebert, Coralie L; Bienvenut, Willy V; Le Caer, Jean-Pierre; Steyaert, Jean-Marc; Giglione, Carmela; Meinnel, Thierry.
Nat Chem Biol; 14(7): 671-679, 2018 07.
Artigo em Inglês | MEDLINE | ID: mdl-29892081
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.
Selo DaSilva