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.
Lisa Schroer
Doctoral Research Fellow
-
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
Publications
-
Davydova, Erna; Shimazu, Tadahiro; Schuhmacher, Maren Kirstin; Jakobsson, Magnus E.; Willemen, Hanneke L.D.M. & Liu, Tongri [Show all 28 contributors for this article] (2021). The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes. Nature Communications. ISSN 2041-1723. 12, p. 1–14. doi: 10.1038/s41467-020-20670-7. Full text in Research Archive
Published Feb. 5, 2019 11:51 AM
- Last modified May 3, 2022 10:30 AM