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[HEMK-Like Methyltransferases in the Regulation of Cellular Processes]
N S Biziaev1, A V Shuvalov1,2, E Z Alkalaeva1,2,3
1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia.
Molekuliarnaia Biologiia
|May 27, 2022
Summary
Human methyltransferase HEMK2 is a multifunctional enzyme. It methylates diverse substrates, including eukaryotic release factor 1 (eRF1), impacting protein biosynthesis across species.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Human methyltransferase (methylase) HEMK2 is a versatile enzyme found across prokaryotes and eukaryotes.
- HEMK2 methylates diverse substrates, including protein residues, DNA, and arsenicals.
Purpose of the Study:
- To review the features of human HEMK2 methylase and its orthologs.
- To highlight their role as multifunctional enzymes regulating cellular processes, particularly protein biosynthesis.
Main Methods:
- Literature review of HEMK2 methylase and its orthologs.
- Analysis of conserved methylation patterns in release factors.
Main Results:
- HEMK2 methylates a key glutamine residue in the GGQ motif of eukaryotic release factor 1 (eRF1).
- This methylation is conserved in eukaryotes, archaea, and bacteria, despite variations in release factor structure.
Conclusions:
- HEMK2 and its orthologs are crucial for regulating protein biosynthesis through conserved methylation mechanisms.
- Understanding HEMK2's multifunctional nature provides insights into fundamental cellular processes.
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