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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2021
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oai:doaj.org-article:f285ea6c5c6e4717b078c180ed9b6cd52021-12-02T13:30:15ZThe methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes10.1038/s41467-020-20670-72041-1723https://doaj.org/article/f285ea6c5c6e4717b078c180ed9b6cd52021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20670-7https://doaj.org/toc/2041-1723Only 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.Erna DavydovaTadahiro ShimazuMaren Kirstin SchuhmacherMagnus E. JakobssonHanneke L. D. M. WillemenTongri LiuAnders MoenAngela Y. Y. HoJędrzej MałeckiLisa SchroerRita PintoTakehiro SuzukiIda A. GrønsbergYoshihiro SohtomeMai AkakabeSara WeirichMasaki KikuchiJesper V. OlsenNaoshi DohmaeTakashi UmeharaMikiko SodeokaValentina SiinoMichael A. McDonoughNiels EijkelkampChristopher J. SchofieldAlbert JeltschYoichi ShinkaiPål Ø. FalnesNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021) |
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Science Q 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 |
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. |
format |
article |
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 |
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 Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/f285ea6c5c6e4717b078c180ed9b6cd5 |
work_keys_str_mv |
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