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We began analyzing https://www.nature.com/articles/cr201755, but it redirected us to https://www.nature.com/articles/cr201755. The analysis below is for the second page.

Title[redir]:
5-methylcytosine promotes mRNA export — NSUN2 as the methyltransferase and ALYREF as an m5C reader | Cell Research
Description:
5-methylcytosine (m5C) is a post-transcriptional RNA modification identified in both stable and highly abundant tRNAs and rRNAs, and in mRNAs. However, its regulatory role in mRNA metabolism is still largely unknown. Here, we reveal that m5C modification is enriched in CG-rich regions and in regions immediately downstream of translation initiation sites and has conserved, tissue-specific and dynamic features across mammalian transcriptomes. Moreover, m5C formation in mRNAs is mainly catalyzed by the RNA methyltransferase NSUN2, and m5C is specifically recognized by the mRNA export adaptor ALYREF as shown by in vitro and in vivo studies. NSUN2 modulates ALYREF

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Keywords {🔍}

mrna, sites, rna, figure, article, mrnas, alyref, information, google, scholar, nsun, supplementary, export, cas, cells, cell, nuclear, min, mouse, analysis, buffer, modification, protein, hela, nature, rnabisseq, performed, methylation, human, binding, cytoplasmic, distribution, data, modifications, tissues, samples, levels, line, sigma, identified, sequence, level, regions, gene, quantification, biol, yang, dynamic, rnas, specific,

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nature portfolio privacy policy mononucleoside uhplc-mrm-ms/ms analysis purified pcdna3-t7-ha-dhfr plasmid uhplc-mrm-ms/ms chromatograms advertising uhplc-mrm-ms/ms approach uhplc-mrm-ms/ms analysis pcmv6-entry-alyref-myc-ddk fisher scientific applied uhplc-mrm-ms/ms performed uhplc-mrm-ms/ms egfp/gfp-tagged wild-type social media dynamic nature cell research website reversible nature uhplc-mrm-ms/ms n6-methyladenosine-dependent regulation 0/ reprints immune microenvironment-related characteristics yun-gui yang gui-bin jiang methylation-individual-nucleotide-resolution crosslinking aly/ref export factor streptavidin-conjugated magnetic beads research center high-throughput sequencing data nxf1-nxt1 heterodimer binds flag-tagged human nsun1 full size image nature 2012 nature 2014 nature 2015 nature 2016 nature 2000 nature alyref-dependent pathway serves rna-bisseq data sets biotin-labeled rna oligonucleotides medical research undergo nuclear-cytoplasmic shuttling dynamic n1-methyladenosine methylome rescue par-clip assay purified flag-alyref protein flag-alyref wild-type real-time quantitative pcr anti-alyref polyclonal antibody library collecting alyref-mediated mrna export

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         description:5-methylcytosine (m5C) is a post-transcriptional RNA modification identified in both stable and highly abundant tRNAs and rRNAs, and in mRNAs. However, its regulatory role in mRNA metabolism is still largely unknown. Here, we reveal that m5C modification is enriched in CG-rich regions and in regions immediately downstream of translation initiation sites and has conserved, tissue-specific and dynamic features across mammalian transcriptomes. Moreover, m5C formation in mRNAs is mainly catalyzed by the RNA methyltransferase NSUN2, and m5C is specifically recognized by the mRNA export adaptor ALYREF as shown by in vitro and in vivo studies. NSUN2 modulates ALYREF's nuclear-cytoplasmic shuttling, RNA-binding affinity and associated mRNA export. Dysregulation of ALYREF-mediated mRNA export upon NSUN2 depletion could be restored by reconstitution of wild-type but not methyltransferase-defective NSUN2. Our study provides comprehensive m5C profiles of mammalian transcriptomes and suggests an essential role for m5C modification in mRNA export and post-transcriptional regulation.
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      headline:5-methylcytosine promotes mRNA export â NSUN2 as the methyltransferase and ALYREF as an m5C reader
      description:5-methylcytosine (m5C) is a post-transcriptional RNA modification identified in both stable and highly abundant tRNAs and rRNAs, and in mRNAs. However, its regulatory role in mRNA metabolism is still largely unknown. Here, we reveal that m5C modification is enriched in CG-rich regions and in regions immediately downstream of translation initiation sites and has conserved, tissue-specific and dynamic features across mammalian transcriptomes. Moreover, m5C formation in mRNAs is mainly catalyzed by the RNA methyltransferase NSUN2, and m5C is specifically recognized by the mRNA export adaptor ALYREF as shown by in vitro and in vivo studies. NSUN2 modulates ALYREF's nuclear-cytoplasmic shuttling, RNA-binding affinity and associated mRNA export. Dysregulation of ALYREF-mediated mRNA export upon NSUN2 depletion could be restored by reconstitution of wild-type but not methyltransferase-defective NSUN2. Our study provides comprehensive m5C profiles of mammalian transcriptomes and suggests an essential role for m5C modification in mRNA export and post-transcriptional regulation.
      datePublished:2017-04-18T00:00:00Z
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         Transcription
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         Transferases
         m5C
         mRNA export
         ALYREF
         NSUN2
         Life Sciences
         general
         Cell Biology
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      name:School of Life Science, University of Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:School of Life Science, University of Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:School of Life Science, University of Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:National Institute of Biological Sciences, Beijing, China
      name:State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing, China
      name:Center for Reproductive Medicine, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, China
      name:Key Laboratory of Genomic and Precision Medicine, Collaborative Innovation Center of Genetics and Development, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, China
      name:School of Life Science, University of Chinese Academy of Sciences, Beijing, China

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