Human cap methyltransferase (RNMT) N-terminal non-catalytic domain mediates recruitment to transcription initiation sites

Michael Aregger, Victoria H. Cowling

    Research output: Contribution to journalArticle

    16 Citations (Scopus)

    Abstract

    Gene expression in eukaryotes is dependent on the mRNA methyl cap which mediates mRNA processing and translation initiation. Synthesis of the methyl cap initiates with addition of 7-methylguanosine to the initiating nucleotide of RNA pol II transcripts, which occurs predominantly during transcription and in mammals is catalyzed by RNGTT (RNA guanylyltransferase and 5' phosphatase) and RNMT (RNA guanine-7 methyltransferase). RNMT has a methyltransferase domain and an N-terminal domain whose function is unclear; it is conserved in mammals but not required for cap methyltransferase activity. We report that the RNMT N-terminal domain is necessary and sufficient for RNMT recruitment to transcription initiation sites and that recruitment occurs in a DRB-dependent manner. The RNMT-activating subunit, RAM, is also recruited to transcription initiation sites via an interaction with RNMT. The RNMT N-terminal domain is required for transcript expression, translation and cell proliferation.
    Original languageEnglish
    Pages (from-to)67-73
    Number of pages7
    JournalBiochemical Journal
    Volume455
    Issue number1
    DOIs
    Publication statusPublished - 18 Jul 2013

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  • Student Theses

    Cell cycle-dependent regulation of the human RNA cap methyltransferase (RNMT)

    Author: Aregger, M., 2013

    Supervisor: Cowling, V. (Supervisor)

    Student thesis: Doctoral ThesisDoctor of Philosophy

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