Sebastian Kwiatkowski and Jakub Drozak * Pages 1 - 15 ( 15 )
Protein histidine methylation is rarely studied posttranslational modification in eukaryotes. Although the presence of N-methylhistidine residue in actin has been demonstrated in early 1960s, only a very limited number of methylhistidine-containing proteins including S100A9, myosin, myosin kinase and ribosomal protein RPL3 have been reported to date. The role of histidine methylation in protein function and in cell physiology also remain largely uncharted mostly due to a shortage of studies focusing on these issues. Recently, however, molecular identities of first two distinct histidine-specific protein methyltransferases have been established in yeast (Hpm1) and in metazoan (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 function whose loss may have deleterious consequences on both cells and organisms. This review aims to summarize the recent advances in the understanding of the chemical, enzymological and physiological aspects of protein histidine methylation.
post-translational modification, protein methylation, histidine methylation, actin, SETD3, Hpm1
Department of Metabolic Regulation, Faculty of Biology, University of Warsaw, Miecznikowa 1 , Department of Metabolic Regulation, Faculty of Biology, University of Warsaw, Miecznikowa 1