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Keywords
- Analysis of RNA Modifications (1)
- Barbituric Acid Merocyanines (1)
- Crystal structure of MTR1 (1)
- DNA catalyst (1)
- DNA-based nanostructures (1)
- DNA-processing enzymes (1)
- High-Throughput Sequencing Method, DZ-seq (1)
- Higher-order Transient Absorption Spectroscopy (1)
- Methyltransferase Ribozyme (1)
- Methyltransferase Ribozyme MTR1 (1)
Institute
Sonstige beteiligte Institutionen
- International Max Planck Research School Molecular Biology, University of Göttingen, Germany (2)
- Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), Göttingen, Germany (1)
- Center for Nanosystems Chemistry (CNC), University of Würzburg (1)
- Department of Molecular Biology, University Medical Center Göttingen, Germany (1)
- Department of Molecular Biology, University Medical Centre Göttingen, Göttingen 37073, Germany (1)
- Göttingen Center for Molecular Biosciences, Georg- August University Göttingen, Göttingen 37077, Germany (1)
EU-Project number / Contract (GA) number
- 682586 (7)
RNA-catalysed RNA methylation was recently shown to be part of the catalytic repertoire of ribozymes. The methyltransferase ribozyme MTR1 catalyses the site-specific synthesis of 1-methyladenosine (m\(^1\)A) in RNA, using O\(^6\)-methylguanine (m\(^6\)G) as methyl group donor. Here we report the crystal structure of MTR1 at a resolution of 2.8 Å, which reveals a guanine binding site reminiscent of natural guanine riboswitches. The structure represents the postcatalytic state of a split ribozyme in complex with the m1A-containing RNA product and the demethylated cofactor guanine. The structural data suggest the mechanistic involvement of a protonated cytidine in the methyl transfer reaction. A synergistic effect of two 2'-O-methylated ribose residues in the active site results in accelerated methyl group transfer. Supported by these results, it seems plausible that modified nucleotides may have enhanced early RNA catalysis and that metabolite-binding riboswitches may resemble inactivated ribozymes that have lost their catalytic activity during evolution.