2. Academic Validation
  3. Characterization of hMTr1, a human Cap1 2'-O-ribose methyltransferase

Characterization of hMTr1, a human Cap1 2'-O-ribose methyltransferase

  • J Biol Chem. 2010 Oct 22;285(43):33037-33044. doi: 10.1074/jbc.M110.155283.
François Bélanger 1,  Janusz Stepinski 2,  Edward Darzynkiewicz 2,  Jerry Pelletier 3
Affiliations

Affiliations

  • 1 From the Departments of Biochemistry and Oncology and The Rosalind and Morris Goodman Cancer Research Center, McGill University, Montreal, Quebec H3G 1Y6, Canada.
  • 2 Division of Biophysics, Institute of Experimental Physics, Faculty of Physics, University of Warsaw, 02-089 Warsaw, Poland.
  • 3 From the Departments of Biochemistry and Oncology and The Rosalind and Morris Goodman Cancer Research Center, McGill University, Montreal, Quebec H3G 1Y6, Canada. Electronic address: jerry.pelletier@mcgill.ca.
PMID: 20713356 DOI: 10.1074/jbc.M110.155283
Abstract

Cellular eukaryotic mRNAs are capped at their 5' ends with a 7-methylguanosine nucleotide, a structural feature that has been shown to be important for conferring mRNA stability, stimulating mRNA biogenesis (splicing, poly(A) addition, nucleocytoplasmic transport), and increasing translational efficiency. Whereas yeast mRNAs have no additional modifications to the cap, called cap0, higher eukaryotes are methylated at the 2'-O-ribose of the first or the first and second transcribed nucleotides, called cap1 and cap2, respectively. In the present study, we identify the methyltransferase responsible for cap1 formation in human cells, which we call hMTr1 (also known as FTSJD2 and ISG95). We show in vitro that hMTr1 catalyzes specific methylation of the 2'-O-ribose of the first nucleotide of a capped RNA transcript. Using siRNA-mediated knockdown of hMTr1 in HeLa cells, we demonstrate that hMTr1 is responsible for cap1 formation in vivo.

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