Protein Histidine Methylation

Sebastian	      Kwiatkowski; Jakub	      Drozak
doi:10.2174/1389203721666200318161330
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.
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DOI https://dx.doi.org/10.2174/1389203721666200318161330	Print ISSN 1389-2037
Publisher Name Bentham Science Publisher	Online ISSN 1875-5550
Current Protein & Peptide Science

Protein Histidine Methylation

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