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c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production

The mRNA cap is a structure added to RNA pol II transcripts in eukaryotes, which recruits factors involved in RNA processing, nuclear export and translation initiation. RNA guanine-7 methyltransferase (RNMT)–RNA-activating miniprotein (RAM), the mRNA cap methyltransferase complex, completes the basi...

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Detalles Bibliográficos
Autores principales: Dunn, Sianadh, Lombardi, Olivia, Cowling, Victoria H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5247799/
https://www.ncbi.nlm.nih.gov/pubmed/27934633
http://dx.doi.org/10.1042/BCJ20160930
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author Dunn, Sianadh
Lombardi, Olivia
Cowling, Victoria H.
author_facet Dunn, Sianadh
Lombardi, Olivia
Cowling, Victoria H.
author_sort Dunn, Sianadh
collection PubMed
description The mRNA cap is a structure added to RNA pol II transcripts in eukaryotes, which recruits factors involved in RNA processing, nuclear export and translation initiation. RNA guanine-7 methyltransferase (RNMT)–RNA-activating miniprotein (RAM), the mRNA cap methyltransferase complex, completes the basic functional mRNA cap structure, cap 0, by methylating the cap guanosine. Here, we report that RNMT–RAM co-ordinates mRNA processing with ribosome production. Suppression of RNMT–RAM reduces synthesis of the 45S ribosomal RNA (rRNA) precursor. RNMT–RAM is required for c-Myc expression, a major regulator of RNA pol I, which synthesises 45S rRNA. Constitutive expression of c-Myc restores rRNA synthesis when RNMT–RAM is suppressed, indicating that RNMT–RAM controls rRNA production predominantly by controlling c-Myc expression. We report that RNMT–RAM is recruited to the ribosomal DNA locus, which may contribute to rRNA synthesis in certain contexts.
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spelling pubmed-52477992017-02-02 c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production Dunn, Sianadh Lombardi, Olivia Cowling, Victoria H. Biochem J Research Articles The mRNA cap is a structure added to RNA pol II transcripts in eukaryotes, which recruits factors involved in RNA processing, nuclear export and translation initiation. RNA guanine-7 methyltransferase (RNMT)–RNA-activating miniprotein (RAM), the mRNA cap methyltransferase complex, completes the basic functional mRNA cap structure, cap 0, by methylating the cap guanosine. Here, we report that RNMT–RAM co-ordinates mRNA processing with ribosome production. Suppression of RNMT–RAM reduces synthesis of the 45S ribosomal RNA (rRNA) precursor. RNMT–RAM is required for c-Myc expression, a major regulator of RNA pol I, which synthesises 45S rRNA. Constitutive expression of c-Myc restores rRNA synthesis when RNMT–RAM is suppressed, indicating that RNMT–RAM controls rRNA production predominantly by controlling c-Myc expression. We report that RNMT–RAM is recruited to the ribosomal DNA locus, which may contribute to rRNA synthesis in certain contexts. Portland Press Ltd. 2017-02-01 2017-01-20 /pmc/articles/PMC5247799/ /pubmed/27934633 http://dx.doi.org/10.1042/BCJ20160930 Text en © 2017 The Author(s) https://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (https://creativecommons.org/licenses/by/4.0) .
spellingShingle Research Articles
Dunn, Sianadh
Lombardi, Olivia
Cowling, Victoria H.
c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production
title c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production
title_full c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production
title_fullStr c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production
title_full_unstemmed c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production
title_short c-Myc co-ordinates mRNA cap methylation and ribosomal RNA production
title_sort c-myc co-ordinates mrna cap methylation and ribosomal rna production
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5247799/
https://www.ncbi.nlm.nih.gov/pubmed/27934633
http://dx.doi.org/10.1042/BCJ20160930
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