Methyltransferases (MTases) have mostly been known to target lysine residues as post-translational protein modification. However, some are proven to target histidine residues. Histidine can be methylated on the π- or τ-nitrogen. So far, only five mammalian proteins have been identified as substrate of such MTase. During my PhD, I will focus on the identification of histidine MTases and their substrates as well as the dynamic regulation and function.
- Davydova, Erna; Shimazu, Tadahiro; Schuhmacher, Maren Kirstin; Jakobsson, Magnus E.; Willemen, Hanneke L.D.M.; Liu, Tongri; Moen, Anders; Ho, Angela Yeuan Yen; Malecki, Jedrzej Mieczyslaw; Schroer, Lisa; Pinto, Rita; Suzuki, Takehiro; Grønsberg, Ida A.; Sohtome, Yoshihiro; Akakabe, Mai; Weirich, Sara; Kikuchi, Masaki; Olsen, Jesper V.; Dohmae, Naoshi; Umehara, Takashi; Sodeoka, Mikiko; Siino, Valentina; McDonough, Michael A.; Eijkelkamp, Niels; Schofield, Christopher J.; Jeltsch, Albert; Shinkai, Yoichi & Falnes, Pål Øystein (2021). The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes. Nature Communications. ISSN 2041-1723. 12:891, s 1- 14 . doi: 10.1038/s41467-020-20670-7