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@article{Trainor:2024:10.1038/s42004-024-01227-x,
author = {Trainor, N and Whitwell, H and Jimenez, B and Addison, K and Leonidou, E and DiMaggio, P and Fuchter, M},
doi = {10.1038/s42004-024-01227-x},
journal = {Communications Chemistry},
title = {Tracking DOT1L methyltransferase activity by stable isotope labelling using a selective synthetic co-factor},
url = {http://dx.doi.org/10.1038/s42004-024-01227-x},
volume = {7},
year = {2024}
}
TY - JOUR
AB - Epigenetic processes influence health and disease through mechanisms which alter gene expression. In contrast to genetic changes which affect DNA sequences, epigenetic marks include DNA base modifications or post-translational modification (PTM) of proteins. Histone methylation is a prominent and versatile example of an epigenetic marker: gene expression or silencing is dependent on the location and extent of the methylation. Protein methyltransferases exhibit functional redundancy and broad preferences for multiple histone residues, which presents a challenge for the study of their individual activities. We developed an isotopically labelled analogue of co-factor S-adenosyl-L-methionine (13CD3-BrSAM), with selectivity for the histone lysine methyltransferase DOT1L, permitting tracking of methylation activity by mass spectrometry (MS). This concept could be applied to other methyltransferases, linking PTM discovery to enzymatic mediators.
AU - Trainor,N
AU - Whitwell,H
AU - Jimenez,B
AU - Addison,K
AU - Leonidou,E
AU - DiMaggio,P
AU - Fuchter,M
DO - 10.1038/s42004-024-01227-x
PY - 2024///
SN - 2399-3669
TI - Tracking DOT1L methyltransferase activity by stable isotope labelling using a selective synthetic co-factor
T2 - Communications Chemistry
UR - http://dx.doi.org/10.1038/s42004-024-01227-x
UR - https://www.nature.com/articles/s42004-024-01227-x
VL - 7
ER -