The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

Only very few enzymes are known to catalyze protein histidine methylation. Here, the authors show that METTL9 is responsible for most 1-methylhistidine modifications in mouse and human proteomes, and characterize METTL9′s substrate specificity and potential cellular functions.

Bibliographic Details
Main Authors: Erna Davydova, Tadahiro Shimazu, Maren Kirstin Schuhmacher, Magnus E. Jakobsson, Hanneke L. D. M. Willemen, Tongri Liu, Anders Moen, Angela Y. Y. Ho, Jędrzej Małecki, Lisa Schroer, Rita Pinto, Takehiro Suzuki, Ida A. Grønsberg, Yoshihiro Sohtome, Mai Akakabe, Sara Weirich, Masaki Kikuchi, Jesper V. Olsen, Naoshi Dohmae, Takashi Umehara, Mikiko Sodeoka, Valentina Siino, Michael A. McDonough, Niels Eijkelkamp, Christopher J. Schofield, Albert Jeltsch, Yoichi Shinkai, Pål Ø. Falnes
Format: Article
Language:English
Published: Nature Publishing Group 2021-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-20670-7
Description
Summary:Only very few enzymes are known to catalyze protein histidine methylation. Here, the authors show that METTL9 is responsible for most 1-methylhistidine modifications in mouse and human proteomes, and characterize METTL9′s substrate specificity and potential cellular functions.
ISSN:2041-1723

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