Protein Histidine Methylation.
Curr Protein Pept Sci
; 21(7): 675-689, 2020.
Article
en En
| MEDLINE
| ID: mdl-32188384
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.
Palabras clave
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Proteína Metiltransferasas
/
Proteínas Ribosómicas
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Quinasa de Cadena Ligera de Miosina
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Procesamiento Proteico-Postraduccional
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Actinas
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Histidina
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Curr Protein Pept Sci
Asunto de la revista:
BIOQUIMICA
Año:
2020
Tipo del documento:
Article
País de afiliación:
Polonia