ArticleThe Journal of biological chemistry2015
UPF0586 Protein C9orf41 Homolog Is Anserine-producing Methyltransferase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 53 citations in OpenAlex.
- Carnosinylation of Cardiac Antigens Attenuates Immunogenic Responses and Improves Function in Failing Hearts.Journal of the American Heart Association · 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
- Replacing Soybean Meal with Hemp Leaves in a Dairy Cow Diet: Plasma Antioxidative Capacity, Inflammatory Parameters and Milk Constituents.Animals : an open access journal from MDPI · 2025Article
- Functional genetics reveals modulators of antimicrotubule drug sensitivity.The Journal of cell biology · 2025Article
- Article
- Review
- Closing in on human methylation-the versatile family of seven-β-strand (METTL) methyltransferases.Nucleic acids research · 2024Review
- Metabolic pathways for removing reactive aldehydes are diminished in the skeletal muscle during heart failure.Skeletal muscle · 2024Article
- Metabolic labeling based methylome profiling enables functional dissection of histidine methylation in C3H1 zinc fingers.Nature communications · 2024Article
- Genome-wide association studies of anserine and carnosine contents in the breast meat of Korean native chickens.Poultry science · 2024Article
- An evolutionary mechanism to assimilate new nutrient sensors into the mTORC1 pathway.Nature communications · 2024Article
- Functional genetics reveals modulators of anti-microtubule drug sensitivity.bioRxiv : the preprint server for biology · 2024Article
- Metabolic Pathways for Removing Reactive Aldehydes are Diminished in Atrophic Muscle During Heart Failure.Research square · 2023Article
- Histidine N1-position-specific methyltransferase CARNMT1 targets C3H zinc finger proteins and modulates RNA metabolism.Genes & development · 2023Article
- Putting a finger on histidine methylation.Genes & development · 2023Article
- The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular basis for protein histidine N1-specific methylation of the "His-x-His" motifs by METTL9.Cell insight · 2023Article
- An evolutionary mechanism to assimilate new nutrient sensors into the mTORC1 pathway.bioRxiv : the preprint server for biology · 2023Article
- Proteomics-based trapping with single or multiple inactive mutants reproducibly profiles histone deacetylase 1 substrates.Journal of proteomics · 2023Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Anserine (β-alanyl-N(Pi)-methyl-L-histidine), a methylated derivative of carnosine (β-alanyl-L-histidine), is an abundant constituent of vertebrate skeletal muscles. Although it has been suggested to serve as a proton buffer and radical scavenger, its physiological function remains mysterious. The formation of anserine is catalyzed by carnosine N-methyltransferase, recently identified in chicken as histamine N-methyltransferase-like (HNMT-like) protein. Although the HNMT-like gene is absent in mammalian genomes, the activity of carnosine N-methyltransferase was reported in most mammalian species. In the present investigation, we purified carnosine N-methyltransferase from rat muscles about 2600-fold. Three polypeptides of ∼ 45, 50, and 70 kDa coeluting with the enzyme activity were identified in the preparation. Mass spectrometry analysis of these polypeptides resulted in the identification of UPF0586 protein C9orf41 homolog as the only meaningful candidate. Rat UPF0586 and its yeast, chicken, and human orthologs were expressed in COS-7 cells and purified to homogeneity. Although all recombinant proteins catalyzed the formation of anserine, as confirmed by chromatographic and mass spectrometry analysis, rat UPF0586 was more active on carnosine than other orthologs. Confocal microscopy of HeLa cells expressing recombinant UPF5086 proteins revealed their presence in both cytosol and nucleus. Carnosine and Gly-His were the best substrates for all UPF0586 orthologs studied, although the enzymes also methylated other l-histidine-containing di- and tripeptides. Finally, cotransfection of COS-7 cells with rat or human UPF0586 and carnosine synthase transformed the cells into efficient anserine producers. We conclude that UPF0586 is mammalian carnosine N-methyltransferase and hypothesize that it may also serve as a peptide or protein methyltransferase in eukaryotes.
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