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.
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2021-02-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-020-20670-7 |
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doaj-f285ea6c5c6e4717b078c180ed9b6cd52021-02-14T12:13:01ZengNature Publishing GroupNature Communications2041-17232021-02-0112111410.1038/s41467-020-20670-7The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomesErna Davydova0Tadahiro Shimazu1Maren Kirstin Schuhmacher2Magnus E. Jakobsson3Hanneke L. D. M. Willemen4Tongri Liu5Anders Moen6Angela Y. Y. Ho7Jędrzej Małecki8Lisa Schroer9Rita Pinto10Takehiro Suzuki11Ida A. Grønsberg12Yoshihiro Sohtome13Mai Akakabe14Sara Weirich15Masaki Kikuchi16Jesper V. Olsen17Naoshi Dohmae18Takashi Umehara19Mikiko Sodeoka20Valentina Siino21Michael A. McDonough22Niels Eijkelkamp23Christopher J. Schofield24Albert Jeltsch25Yoichi Shinkai26Pål Ø. Falnes27Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloCellular Memory Laboratory, RIKEN Cluster for Pioneering Research, WakoDepartment of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of StuttgartProteomics Program, Faculty of Health and Medical Sciences, Novo Nordisk Foundation Center for Protein Research (NNF-CPR), University of CopenhagenCenter for Translational Immunology (CTI), University Medical Center Utrecht, Utrecht UniversityChemistry Research Laboratory, Department of Chemistry, University of OxfordDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloBiomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, WakoDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, WakoSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, WakoDepartment of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of StuttgartLaboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics ResearchProteomics Program, Faculty of Health and Medical Sciences, Novo Nordisk Foundation Center for Protein Research (NNF-CPR), University of CopenhagenBiomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science, WakoLaboratory for Epigenetics Drug Discovery, RIKEN Center for Biosystems Dynamics ResearchSynthetic Organic Chemistry Laboratory, RIKEN Cluster for Pioneering Research, WakoDepartment of Immunotechnology, Lund UniversityChemistry Research Laboratory, Department of Chemistry, University of OxfordCenter for Translational Immunology (CTI), University Medical Center Utrecht, Utrecht UniversityChemistry Research Laboratory, Department of Chemistry, University of OxfordDepartment of Biochemistry, Institute of Biochemistry and Technical Biochemistry, University of StuttgartCellular Memory Laboratory, RIKEN Cluster for Pioneering Research, WakoDepartment of Biosciences, Faculty of Mathematics and Natural Sciences, University of OsloOnly 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.https://doi.org/10.1038/s41467-020-20670-7 |
| collection |
DOAJ |
| language |
English |
| format |
Article |
| sources |
DOAJ |
| author |
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 |
| spellingShingle |
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 The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes Nature Communications |
| author_facet |
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 |
| author_sort |
Erna Davydova |
| title |
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes |
| title_short |
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes |
| title_full |
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes |
| title_fullStr |
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes |
| title_full_unstemmed |
The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes |
| title_sort |
methyltransferase mettl9 mediates pervasive 1-methylhistidine modification in mammalian proteomes |
| publisher |
Nature Publishing Group |
| series |
Nature Communications |
| issn |
2041-1723 |
| publishDate |
2021-02-01 |
| description |
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. |
| url |
https://doi.org/10.1038/s41467-020-20670-7 |
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