Lisa Schroer
Doctoral Research Fellow
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Section for Biochemistry and Molecular Biology
Norwegian version of this page
Email
lisa.schroer@ibv.uio.no
Room
2102A
Username
Visiting address
Kristine Bonnevies hus
Blindernveien 31
0371 Oslo
Postal address
Postboks 1066 Blindern
0316 Oslo
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.
Publications
- 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
Published Feb. 5, 2019 11:51 AM
- Last modified Jan. 29, 2020 10:55 AM