Structural analysis of human 2′-O-ribose methyltransferases involved in mRNA cap structure formation

Miroslaw Smietanski, Maria Werner, Elzbieta Purta, Katarzyna H. Kaminska, Janusz Stepinski, Edward Darzynkiewicz, Marcin Nowotny () and Janusz M. Bujnicki ()
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Miroslaw Smietanski: Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw
Maria Werner: Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw
Elzbieta Purta: Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw
Katarzyna H. Kaminska: Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw
Janusz Stepinski: Institute of Experimental Physics, Faculty of Physics, University of Warsaw
Edward Darzynkiewicz: Institute of Experimental Physics, Faculty of Physics, University of Warsaw
Marcin Nowotny: Laboratory of Protein Structure, International Institute of Molecular and Cell Biology in Warsaw
Janusz M. Bujnicki: Laboratory of Bioinformatics and Protein Engineering, International Institute of Molecular and Cell Biology in Warsaw

Nature Communications, 2014, vol. 5, issue 1, 1-10

Abstract: Abstract The 5′ cap of human messenger RNA contains 2′-O-methylation of the first and often second transcribed nucleotide that is important for its processing, translation and stability. Human enzymes that methylate these nucleotides, termed CMTr1 and CMTr2, respectively, have recently been identified. However, the structures of these enzymes and their mechanisms of action remain unknown. In the present study, we solve the crystal structures of the active CMTr1 catalytic domain in complex with a methyl group donor and a capped oligoribonucleotide, thereby revealing the mechanism of specific recognition of capped RNA. This mechanism differs significantly from viral enzymes, thus providing a framework for their specific targeting. Based on the crystal structure of CMTr1, a comparative model of the CMTr2 catalytic domain is generated. This model, together with mutational analysis, leads to the identification of residues involved in RNA and methyl group donor binding.

Date: 2014
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DOI: 10.1038/ncomms4004

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