PTMScan® Methyl Histidine Motif (me-H) Kit #68811
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Background
Early studies identified actin and myosin, isolated from skeletal muscle, as protein substrates containing me-H (2). Due to the abundance of this PTM in muscle tissue, the measurement of free me-H excreted in urine has been proposed as a biomarker of muscle breakdown and turnover (3,4). Additional non-cytoskeletal substrates include histones (5) and the large ribosomal subunit protein (6,7). Both the human and Saccharomyces cerevisiae homologs of the large ribosomal subunit protein contain a conserved histidine residue (RPL3 H245 and Rpl3 H243, respectively) that is methylated by METTL18 and Hpm1, respectively. Methylation on the histidine residue blocks hydrogen bond formation with the 28S rRNA subunit, which may affect overall ribosomal structure and translation efficiency.
Despite the identification of me-H sites on some abundant proteins, such as actin, proteomics studies estimate that the number of histidine methylation sites is less than the number of lysine or arginine methylation sites (8). The elucidation of me-H sites, as well as the enzymes that regulate this PTM, remain an area of active research (9).
- (1984) Biochem J 219, 345-73.
- Johnson, P. et al. (1967) Biochem J 105, 361-70.
- Long, C.L. et al. (1975) Metabolism 24, 929-35.
- Bilmazes, C. et al. (1978) Metabolism 27, 525-30.
- Hayashi, T. et al. (2023) J Biol Chem 299, 105131.
- Al-Hadid, Q. et al. (2014) Mol Cell Biol 34, 2903-16.
- Matsuura-Suzuki, E. et al. (2022) Elife 11, e72780. doi: 10.7554/eLife.72780.
- Kapell, S. and Jakobsson, M.E. (2021) NAR Genom Bioinform 3, lqab045.
- Wang, X. et al. (2023) Cell Discov 9, 38.
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