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Nat Commun ; 12(1): 891, 2021 02 09.
Artigo em Inglês | MEDLINE | ID: mdl-33563959

RESUMO

Post-translational methylation plays a crucial role in regulating and optimizing protein function. Protein histidine methylation, occurring as the two isomers 1- and 3-methylhistidine (1MH and 3MH), was first reported five decades ago, but remains largely unexplored. Here we report that METTL9 is a broad-specificity methyltransferase that mediates the formation of the majority of 1MH present in mouse and human proteomes. METTL9-catalyzed methylation requires a His-x-His (HxH) motif, where "x" is preferably a small amino acid, allowing METTL9 to methylate a number of HxH-containing proteins, including the immunomodulatory protein S100A9 and the NDUFB3 subunit of mitochondrial respiratory Complex I. Notably, METTL9-mediated methylation enhances respiration via Complex I, and the presence of 1MH in an HxH-containing peptide reduced its zinc binding affinity. Our results establish METTL9-mediated 1MH as a pervasive protein modification, thus setting the stage for further functional studies on protein histidine methylation.


Assuntos
Metilistidinas/metabolismo , Metiltransferases/metabolismo , Proteoma/metabolismo , Motivos de Aminoácidos , Animais , Células Cultivadas , Histidina/metabolismo , Humanos , Mamíferos/classificação , Mamíferos/genética , Mamíferos/metabolismo , Metilação , Metiltransferases/genética , Camundongos , Camundongos Endogâmicos C57BL , Camundongos Knockout , Mitocôndrias/metabolismo , Mutação , Processamento de Proteína Pós-Traducional , Proteoma/química , Especificidade por Substrato , Zinco/metabolismo
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