Protein Histidine Methylation

Author(s): Sebastian Kwiatkowski, Jakub Drozak*

Journal Name: Current Protein & Peptide Science

Volume 21 , Issue 7 , 2020

Become EABM
Become Reviewer
Call for Editor

Graphical Abstract:


Protein histidine methylation is a rarely studied posttranslational modification in eukaryotes. Although the presence of N-methylhistidine was demonstrated in actin in the early 1960s, so far, only a limited number of proteins containing N-methylhistidine have been reported, including S100A9, myosin, skeletal muscle myosin light chain kinase (MLCK 2), and ribosomal protein Rpl3. Furthermore, the role of histidine methylation in the functioning of the protein and in cell physiology remains unclear due to a shortage of studies focusing on this topic. However, the molecular identification of the first two distinct histidine-specific protein methyltransferases has been established in yeast (Hpm1) and in metazoan species (actin-histidine N-methyltransferase), giving new insights into the phenomenon of protein methylation at histidine sites. As a result, we are now beginning to recognize protein histidine methylation as an important regulatory mechanism of protein functioning whose loss may have deleterious consequences in both cells and in organisms. In this review, we aim to summarize the recent advances in the understanding of the chemical, enzymological, and physiological aspects of protein histidine methylation.

Keywords: Posttranslational modifications, protein methylation, histidine methylation, actin, SETD3, Hpm1.

Rights & PermissionsPrintExport Cite as

Article Details

Year: 2020
Published on: 22 September, 2020
Page: [675 - 689]
Pages: 15
DOI: 10.2174/1389203721666200318161330
Price: $65

Article Metrics

PDF: 31