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Vol 56(2022) N 3 p. 395-405; DOI 10.1134/S0026893322030025 Full Text

N.S. Biziaev1, A.V. Shuvalov1,2, E.Z. Alkalaeva1,2*

HEMK-Like Methyltransferases in the Regulation of Cellular Processes

1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia
2Center for Precision Genome Editing and Genetic Technologies for Biomedicine, Moscow, 119991 Russia

*alkalaeva@eimb.ru
Received - 2021-11-26; Revised - 2021-11-26; Accepted - 2021-12-02

Human translational methyltransferase (methylase) HEMK2, whose orthologues are found in many prokaryotes and eukaryotes, methylates such diverse substrates as glutamine and lysine residues in proteins, deoxyadenosine in DNA, and arsenicals. One of the important substrate of HEMK2 methylase is a glutamine residue in the GGQ ultra-conservative motif of the eukaryotic release factor 1 (eRF1). Release factor methylation by HEMK2 orthologs is conserved among eukaryotes, archaea, and bacteria, although bacterial release factors differ in sequence and structure from eukaryotic ones. In this review, we consider the features of human HEMK2 methylase and its orthologs as multifunctional enzymes that regulate cellular processes, in particular, protein biosynthesis.

HEMK2, N6AMT1, eRF1, translation regulation, methylation, post-translational modifications



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