Nature Communications (Feb 2021)
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes
- 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
Affiliations
- Erna Davydova
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- Tadahiro Shimazu
- Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako
- Maren Kirstin Schuhmacher
- Department of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart
- Magnus E. Jakobsson
- Proteomics Program, Faculty of Health and Medical Sciences, Novo Nordisk Foundation Center for Protein Research (NNF-CPR), University of Copenhagen
- Hanneke L. D. M. Willemen
- Center for Translational Immunology (CTI), University Medical Center Utrecht, Utrecht University
- Tongri Liu
- Chemistry Research Laboratory, Department of Chemistry, University of Oxford
- Anders Moen
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- Angela Y. Y. Ho
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- Jędrzej Małecki
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- Lisa Schroer
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- Rita Pinto
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- Takehiro Suzuki
- Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako
- Ida A. Grønsberg
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- Yoshihiro Sohtome
- Synthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako
- Mai Akakabe
- Synthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako
- Sara Weirich
- Department of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart
- Masaki Kikuchi
- Laboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics Research
- Jesper V. Olsen
- Proteomics Program, Faculty of Health and Medical Sciences, Novo Nordisk Foundation Center for Protein Research (NNF-CPR), University of Copenhagen
- Naoshi Dohmae
- Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, Wako
- Takashi Umehara
- Laboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics Research
- Mikiko Sodeoka
- Synthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, Wako
- Valentina Siino
- Department of Immunotechnology, Lund University
- Michael A. McDonough
- Chemistry Research Laboratory, Department of Chemistry, University of Oxford
- Niels Eijkelkamp
- Center for Translational Immunology (CTI), University Medical Center Utrecht, Utrecht University
- Christopher J. Schofield
- Chemistry Research Laboratory, Department of Chemistry, University of Oxford
- Albert Jeltsch
- Department of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of Stuttgart
- Yoichi Shinkai
- Cellular Memory Laboratory, RIKEN Cluster for Pioneering Research, Wako
- Pål Ø. Falnes
- Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo
- DOI
- https://doi.org/10.1038/s41467-020-20670-7
- Journal volume & issue
-
Vol. 12,
no. 1
pp. 1 – 14
Abstract
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.
