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

    15 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

    Fingerprint

    Transcription Initiation Site
    Methyltransferases
    Mammals
    mRNA guanylyltransferase
    Dichlororibofuranosylbenzimidazole
    Messenger RNA
    RNA Polymerase II
    Cell proliferation
    Protein Biosynthesis
    Random access storage
    Transcription
    mRNA (guanine(N7))-methyltransferase
    Eukaryota
    Phosphoric Monoester Hydrolases
    Gene expression
    Nucleotides
    Cell Proliferation
    Gene Expression
    Processing

    Cite this

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    title = "Human cap methyltransferase (RNMT) N-terminal non-catalytic domain mediates recruitment to transcription initiation sites",
    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.",
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    Human cap methyltransferase (RNMT) N-terminal non-catalytic domain mediates recruitment to transcription initiation sites. / Aregger, Michael; Cowling, Victoria H.

    In: Biochemical Journal, Vol. 455, No. 1, 18.07.2013, p. 67-73.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Human cap methyltransferase (RNMT) N-terminal non-catalytic domain mediates recruitment to transcription initiation sites

    AU - Aregger, Michael

    AU - Cowling, Victoria H.

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    AB - 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.

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