ArticleCell insight2023
Molecular basis for protein histidine N1-specific methylation of the "His-x-His" motifs by METTL9.
Article in Cell insight, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Histidine Ethylation by Histidine Methyltransferases SETD3 and METTL9.Chembiochem : a European journal of chemical biology · 2026Article
- Substrate selectivity of human histidine methyltransferase METTL9.Protein science : a publication of the Protein Society · 2026Article
- The Protein Histidine Methyltransferase METTL9-From Mechanism to Biological Function.Life (Basel, Switzerland) · 2026Review
- Review
- Structural and functional analysis of SAM-dependent N-methyltransferases involved in ovoselenol and ovothiol biosynthesis.Structure (London, England : 1993) · 2025Article
- The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK.Cell insight · 2024Article
- Transcriptomic Signatures of the Foetal Liver and Late Prenatal Development in Vitrified Rabbit Embryos.Veterinary sciences · 2024Article
- A novel NCell research · 2023Article
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Authors and funding
7 authors.
Funding
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Abstract
Histidine methylation serves as an intriguing strategy to introduce altered traits of target proteins, including metal ion chelation, histidine-based catalysis, molecular assembly, and translation regulation. As a newly identified histidine methyltransferase, METTL9 catalyzes N1-methylation of protein substrates containing the "His-x-His" motif (HxH, x denotes small side chain residue). Here our structural and biochemical studies revealed that METTL9 specifically methylates the second histidine of the "HxH" motif, while exploiting the first one as a recognition signature. We observed an intimate engagement between METTL9 and a pentapeptide motif, where the small "x" residue is embedded and confined within the substrate pocket. Upon complex formation, the N3 atom of histidine imidazole ring is stabilized by an aspartate residue such that the N1 atom is presented to S-adenosylmethionine for methylation. Moreover, METTL9 displayed a feature in preferred consecutive and "C-to-N" directional methylation of tandem "HxH" repeats that exist in many METTL9 substrates. Collectively, our work illustrates the molecular design of METTL9 in N1-specific methylation of the broadly existing "HxH" motifs, highlighting its importance in histidine methylation biology.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.