Putting a finger on histidine methylation
- Department of Biochemistry and Biophysics, Center for RNA Biology, Center for Biomedical Informatics, Wilmot Cancer Institute, University of Rochester School of Medicine and Dentistry, Rochester, New York 14620, USA
- Corresponding author: paul_boutz{at}urmc.rochester.edu
Abstract
Specialized enzymes add methyl groups to the nitrogens of the amino acid histidine, altering the chemical properties of its imidazole ring and, in turn, the function of the modified (poly)peptide. In this issue of Genes & Development, Shimazu and colleagues (pp. 724–742) make the remarkable discovery that CARNMT1 acts as a dual-specificity histidine methyltransferase, modifying both the small-molecule dipeptide carnosine and a set of proteins, predominantly within RNA-binding C3H zinc finger (C3H ZF) motifs. As a result, CARNMT1 modulates the activity of its protein targets to affect RNA processing and metabolism, ultimately contributing an essential function during mammalian development.
Keywords
- methyltransferase
- CARNMT1
- methylation
- histidine
- mRNA
- splicing
- degradation
- zinc finger protein
- U2AF1
- embryonic lethality
- embryonic development
Footnotes
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Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.351097.123.
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Freely available online through the Genes & Development Open Access option.
This article, published in Genes & Development, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/.
