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Department researcher uncovers orphan PTM

2021-09-09

Cells synthesize proteins from a DNA template and expand their biochemical repertoire through dynamic and enzyme-catalysed post-translational modifications (PTM). Methylation of the amino acid histidine was first reported in the late 1960s but until recently very little was known about its enzymology, extent and function.

 

Dr Magnus Jakobsson and a group international collaborators recently uncovered two completely novel human histidine methylating enzymes, that is METTL18 (PMID: 33693809) and METTL9 (PMID: 33563959). To expand on these enzyme-centric studies they also performed the first system biology study on histidine methylation and revealed that the PTM is widespread across human tissues, cells and subcellular structures (PMID: 34046594).

 

We are only scratching the surface of PTM-mediated protein regulation and slowly beginning to understand its implications in health and disease. The coming years much focus within biomedical protein research will be devoted to comprehending PTMs, and their role in protein regulation. For many diseases, these efforts are anticipated to enable the identification of new therapeutic targets and strategies as well as improved diagnostics.”, says Dr Jakobsson.

 

A Review summarizing the groups recent progress on protein histidine methylation was recently published in the Journal of Biological Chemistry (PMID: 34461099).