FMRP Interacts with C/D Box snoRNA in the Nucleus and Regulates Ribosomal RNA Methylation
FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific set of C/D box snoRNAs in the nucleus. C/D box snoRNAs guide 2'O methylations of ribosomal RNA (rRNA) on defined sites, and this modifica...
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Published in | iScience Vol. 9; pp. 399 - 411 |
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Main Authors | , , , , , , , , , , , , , , , |
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30.11.2018
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Abstract | FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific set of C/D box snoRNAs in the nucleus. C/D box snoRNAs guide 2'O methylations of ribosomal RNA (rRNA) on defined sites, and this modification regulates rRNA folding and assembly of ribosomes. 2'O methylation of rRNA is partial on several sites in human embryonic stem cells, which results in ribosomes with differential methylation patterns. FMRP-snoRNA interaction affects rRNA methylation on several of these sites, and in the absence of FMRP, differential methylation pattern of rRNA is significantly altered. We found that FMRP recognizes ribosomes carrying specific methylation patterns on rRNA and the recognition of methylation pattern by FMRP may potentially determine the translation status of its target mRNAs. Thus, FMRP integrates its function in the nucleus and in the cytoplasm. |
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AbstractList | FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific set of C/D box snoRNAs in the nucleus. C/D box snoRNAs guide 2'O methylations of ribosomal RNA (rRNA) on defined sites, and this modification regulates rRNA folding and assembly of ribosomes. 2'O methylation of rRNA is partial on several sites in human embryonic stem cells, which results in ribosomes with differential methylation patterns. FMRP-snoRNA interaction affects rRNA methylation on several of these sites, and in the absence of FMRP, differential methylation pattern of rRNA is significantly altered. We found that FMRP recognizes ribosomes carrying specific methylation patterns on rRNA and the recognition of methylation pattern by FMRP may potentially determine the translation status of its target mRNAs. Thus, FMRP integrates its function in the nucleus and in the cytoplasm. FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific set of C/D box snoRNAs in the nucleus. C/D box snoRNAs guide 2'O methylations of ribosomal RNA (rRNA) on defined sites, and this modification regulates rRNA folding and assembly of ribosomes. 2'O methylation of rRNA is partial on several sites in human embryonic stem cells, which results in ribosomes with differential methylation patterns. FMRP-snoRNA interaction affects rRNA methylation on several of these sites, and in the absence of FMRP, differential methylation pattern of rRNA is significantly altered. We found that FMRP recognizes ribosomes carrying specific methylation patterns on rRNA and the recognition of methylation pattern by FMRP may potentially determine the translation status of its target mRNAs. Thus, FMRP integrates its function in the nucleus and in the cytoplasm.FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific set of C/D box snoRNAs in the nucleus. C/D box snoRNAs guide 2'O methylations of ribosomal RNA (rRNA) on defined sites, and this modification regulates rRNA folding and assembly of ribosomes. 2'O methylation of rRNA is partial on several sites in human embryonic stem cells, which results in ribosomes with differential methylation patterns. FMRP-snoRNA interaction affects rRNA methylation on several of these sites, and in the absence of FMRP, differential methylation pattern of rRNA is significantly altered. We found that FMRP recognizes ribosomes carrying specific methylation patterns on rRNA and the recognition of methylation pattern by FMRP may potentially determine the translation status of its target mRNAs. Thus, FMRP integrates its function in the nucleus and in the cytoplasm. FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific set of C/D box snoRNAs in the nucleus. C/D box snoRNAs guide 2’O methylations of ribosomal RNA (rRNA) on defined sites, and this modification regulates rRNA folding and assembly of ribosomes. 2’O methylation of rRNA is partial on several sites in human embryonic stem cells, which results in ribosomes with differential methylation patterns. FMRP-snoRNA interaction affects rRNA methylation on several of these sites, and in the absence of FMRP, differential methylation pattern of rRNA is significantly altered. We found that FMRP recognizes ribosomes carrying specific methylation patterns on rRNA and the recognition of methylation pattern by FMRP may potentially determine the translation status of its target mRNAs. Thus, FMRP integrates its function in the nucleus and in the cytoplasm. : Molecular Interaction; Stem Cells Research; Omics Subject Areas: Molecular Interaction, Stem Cells Research, Omics FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific set of C/D box snoRNAs in the nucleus. C/D box snoRNAs guide 2’O methylations of ribosomal RNA (rRNA) on defined sites, and this modification regulates rRNA folding and assembly of ribosomes. 2’O methylation of rRNA is partial on several sites in human embryonic stem cells, which results in ribosomes with differential methylation patterns. FMRP-snoRNA interaction affects rRNA methylation on several of these sites, and in the absence of FMRP, differential methylation pattern of rRNA is significantly altered. We found that FMRP recognizes ribosomes carrying specific methylation patterns on rRNA and the recognition of methylation pattern by FMRP may potentially determine the translation status of its target mRNAs. Thus, FMRP integrates its function in the nucleus and in the cytoplasm. • FMRP binds to C/D Box snoRNAs in the nucleus • Differential 2’O-methylation on rRNA contributes to ribosome heterogeneity in a cell • 2’O-Methylation pattern on ribosomal RNA is altered in the absence of FMRP • FMRP recognizes 2’O-methylation on rRNA, which may determine interaction with ribosomes Molecular Interaction; Stem Cells Research; Omics |
Author | Singh, Randhir Tiwari, Vishal Selvaraj, Bhuvaneish Ramesh, Arati Chattarji, Sumantra D'Souza, Michelle Ninochka Gowda, Naveen Kumar Chandappa Anand, Praveen Dastidar, Sudhriti Ghosh Palakodeti, Dasaradhi Gulyani, Akash Pal, Rakhi Muddashetty, Ravi S. Babu, Rosana Ottakandathil James, Owen G. Chandran, Siddharthan |
AuthorAffiliation | 4 The University of Trans-Disciplinary Health Sciences & Technology (TDU), Bengaluru, Karnataka 560064, India 1 Institute for Stem Cell Biology and Regenerative Medicine, Bengaluru 560065, India 2 National Centre for Biological Sciences, Bengaluru, Karnataka 560065, India 5 Manipal Academy of Higher Education, Madhav Nagar, Manipal, Karnataka 576104, India 3 Centre for Neuroregeneration, University of Edinburgh, Edinburgh EH16 4SB, UK |
AuthorAffiliation_xml | – name: 4 The University of Trans-Disciplinary Health Sciences & Technology (TDU), Bengaluru, Karnataka 560064, India – name: 2 National Centre for Biological Sciences, Bengaluru, Karnataka 560065, India – name: 3 Centre for Neuroregeneration, University of Edinburgh, Edinburgh EH16 4SB, UK – name: 1 Institute for Stem Cell Biology and Regenerative Medicine, Bengaluru 560065, India – name: 5 Manipal Academy of Higher Education, Madhav Nagar, Manipal, Karnataka 576104, India |
Author_xml | – sequence: 1 givenname: Michelle Ninochka surname: D'Souza fullname: D'Souza, Michelle Ninochka – sequence: 2 givenname: Naveen Kumar Chandappa surname: Gowda fullname: Gowda, Naveen Kumar Chandappa – sequence: 3 givenname: Vishal surname: Tiwari fullname: Tiwari, Vishal – sequence: 4 givenname: Rosana Ottakandathil surname: Babu fullname: Babu, Rosana Ottakandathil – sequence: 5 givenname: Praveen surname: Anand fullname: Anand, Praveen – sequence: 6 givenname: Sudhriti Ghosh surname: Dastidar fullname: Dastidar, Sudhriti Ghosh – sequence: 7 givenname: Randhir surname: Singh fullname: Singh, Randhir – sequence: 8 givenname: Owen G. surname: James fullname: James, Owen G. – sequence: 9 givenname: Bhuvaneish surname: Selvaraj fullname: Selvaraj, Bhuvaneish – sequence: 10 givenname: Rakhi surname: Pal fullname: Pal, Rakhi – sequence: 11 givenname: Arati surname: Ramesh fullname: Ramesh, Arati – sequence: 12 givenname: Sumantra surname: Chattarji fullname: Chattarji, Sumantra – sequence: 13 givenname: Siddharthan surname: Chandran fullname: Chandran, Siddharthan – sequence: 14 givenname: Akash surname: Gulyani fullname: Gulyani, Akash – sequence: 15 givenname: Dasaradhi surname: Palakodeti fullname: Palakodeti, Dasaradhi – sequence: 16 givenname: Ravi S. surname: Muddashetty fullname: Muddashetty, Ravi S. |
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Cites_doi | 10.1016/j.molcel.2014.03.023 10.1093/nar/gks698 10.1093/nar/gkw482 10.1371/journal.pgen.1000898 10.1093/hmg/5.8.1083 10.1016/j.cell.2017.05.022 10.1002/ajmg.a.33626 10.1002/wrna.1269 10.1128/MCB.01377-08 10.1523/JNEUROSCI.0937-07.2007 10.1126/science.1118265 10.1016/S1097-2765(00)80012-X 10.1093/nar/gks1007 10.1002/bies.201600264 10.1093/nar/gkw810 10.1146/annurev-pathol-011811-132457 10.1016/j.tibs.2015.07.008 10.1016/S0014-4827(03)00222-2 10.1038/383732a0 10.1261/rna.1528909 10.1002/j.1460-2075.1996.tb00924.x 10.1002/stem.1698 10.1016/j.neuron.2008.10.004 10.1093/nar/gkq776 10.1038/ejhg.2013.311 10.1038/ng0196-91 10.1016/j.ydbio.2012.11.031 10.1134/S0006297916090030 10.1371/journal.pone.0091465 10.1038/nsmb.2939 10.1016/j.molcel.2011.05.006 10.1016/j.molcel.2017.05.021 10.1007/978-1-4939-3792-9_20 10.1038/nrn4001 10.1523/JNEUROSCI.17-05-01539.1997 10.1007/978-1-4939-6807-7_12 |
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References | Collins (10.1016/j.isci.2018.11.007_bib8) 2010; 152A Krogh (10.1016/j.isci.2018.11.007_bib21) 2016; 44 Li (10.1016/j.isci.2018.11.007_bib24) 2014; 32 Lafontaine (10.1016/j.isci.2018.11.007_bib22) 2015; 22 Richter (10.1016/j.isci.2018.11.007_bib33) 2015; 16 Kishore (10.1016/j.isci.2018.11.007_bib20) 2006; 311 Henras (10.1016/j.isci.2018.11.007_bib15) 2015; 6 Khandjian (10.1016/j.isci.2018.11.007_bib18) 1996; 12 Feng (10.1016/j.isci.2018.11.007_bib12) 1997; 1 Chen (10.1016/j.isci.2018.11.007_bib7) 2014; 54 Eberhart (10.1016/j.isci.2018.11.007_bib10) 1996; 5 Simsek (10.1016/j.isci.2018.11.007_bib40) 2017; 169 Incarnato (10.1016/j.isci.2018.11.007_bib16) 2017; 45 Bassell (10.1016/j.isci.2018.11.007_bib3) 2008; 60 Machnicka (10.1016/j.isci.2018.11.007_bib26) 2013; 41 Kim (10.1016/j.isci.2018.11.007_bib19) 2009; 29 Muddashetty (10.1016/j.isci.2018.11.007_bib30) 2011; 42 Shubina (10.1016/j.isci.2018.11.007_bib39) 2016; 81 Marchand (10.1016/j.isci.2018.11.007_bib27) 2017; 1562 Luo (10.1016/j.isci.2018.11.007_bib25) 2010; 6 Bensaddek (10.1016/j.isci.2018.11.007_bib4) 2016; 1455 Myrick (10.1016/j.isci.2018.11.007_bib31) 2014; 22 Feng (10.1016/j.isci.2018.11.007_bib13) 1997; 17 Santoro (10.1016/j.isci.2018.11.007_bib35) 2012; 7 Dong (10.1016/j.isci.2018.11.007_bib9) 2012; 40 Muddashetty (10.1016/j.isci.2018.11.007_bib29) 2007; 27 Taft (10.1016/j.isci.2018.11.007_bib42) 2009; 15 Brameier (10.1016/j.isci.2018.11.007_bib5) 2011; 39 Fridell (10.1016/j.isci.2018.11.007_bib14) 1996; 15 Telias (10.1016/j.isci.2018.11.007_bib44) 2013; 374 Bardoni (10.1016/j.isci.2018.11.007_bib2) 2003; 289 Falaleeva (10.1016/j.isci.2018.11.007_bib11) 2017; 39 Taha (10.1016/j.isci.2018.11.007_bib43) 2014; 9 Sharma (10.1016/j.isci.2018.11.007_bib36) 2015; 40 Shi (10.1016/j.isci.2018.11.007_bib38) 2017; 67 Cavaille (10.1016/j.isci.2018.11.007_bib6) 1996; 383 30763793 - iScience. 2019 Feb 11;12:368 |
References_xml | – volume: 54 start-page: 407 year: 2014 ident: 10.1016/j.isci.2018.11.007_bib7 article-title: Fragile X mental retardation protein regulates translation by binding directly to the ribosome publication-title: Mol. Cell doi: 10.1016/j.molcel.2014.03.023 – volume: 40 start-page: e157 year: 2012 ident: 10.1016/j.isci.2018.11.007_bib9 article-title: RTL-P: a sensitive approach for detecting sites of 2'-O-methylation in RNA molecules publication-title: Nucleic Acids Res. doi: 10.1093/nar/gks698 – volume: 44 start-page: 7884 year: 2016 ident: 10.1016/j.isci.2018.11.007_bib21 article-title: Profiling of 2′-O-Me in human rRNA reveals a subset of fractionally modified positions and provides evidence for ribosome heterogeneity publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkw482 – volume: 6 start-page: e1000898 year: 2010 ident: 10.1016/j.isci.2018.11.007_bib25 article-title: Fragile X mental retardation protein regulates proliferation and differentiation of adult neural stem/progenitor cells publication-title: PLoS Genet. doi: 10.1371/journal.pgen.1000898 – volume: 5 start-page: 1083 year: 1996 ident: 10.1016/j.isci.2018.11.007_bib10 article-title: The fragile X mental retardation protein is a ribonucleoprotein containing both nuclear localization and nuclear export signals publication-title: Hum. Mol. Genet. doi: 10.1093/hmg/5.8.1083 – volume: 169 start-page: 1051 year: 2017 ident: 10.1016/j.isci.2018.11.007_bib40 article-title: The mammalian Ribo-interactome reveals ribosome functional diversity and heterogeneity publication-title: Cell doi: 10.1016/j.cell.2017.05.022 – volume: 152A start-page: 2512 year: 2010 ident: 10.1016/j.isci.2018.11.007_bib8 article-title: Identification of novel FMR1 variants by massively parallel sequencing in developmentally delayed males publication-title: Am. J. Med. Genet. A doi: 10.1002/ajmg.a.33626 – volume: 6 start-page: 225 year: 2015 ident: 10.1016/j.isci.2018.11.007_bib15 article-title: An overview of pre-ribosomal RNA processing in eukaryotes publication-title: Wiley Interdiscip. Rev. RNA doi: 10.1002/wrna.1269 – volume: 29 start-page: 214 year: 2009 ident: 10.1016/j.isci.2018.11.007_bib19 article-title: Fragile X mental retardation protein FMRP binds mRNAs in the nucleus publication-title: Mol. Cell. Biol. doi: 10.1128/MCB.01377-08 – volume: 27 start-page: 5338 year: 2007 ident: 10.1016/j.isci.2018.11.007_bib29 article-title: Dysregulated metabotropic glutamate receptor-dependent translation of AMPA receptor and postsynaptic density-95 mRNAs at synapses in a mouse model of fragile X syndrome publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.0937-07.2007 – volume: 311 start-page: 230 year: 2006 ident: 10.1016/j.isci.2018.11.007_bib20 article-title: The snoRNA HBII-52 regulates alternative splicing of the serotonin receptor 2C publication-title: Science doi: 10.1126/science.1118265 – volume: 1 start-page: 109 year: 1997 ident: 10.1016/j.isci.2018.11.007_bib12 article-title: FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association publication-title: Mol. Cell doi: 10.1016/S1097-2765(00)80012-X – volume: 41 start-page: D262 year: 2013 ident: 10.1016/j.isci.2018.11.007_bib26 article-title: MODOMICS: a database of RNA modification pathways–2013 update publication-title: Nucleic Acids Res. doi: 10.1093/nar/gks1007 – volume: 39 year: 2017 ident: 10.1016/j.isci.2018.11.007_bib11 article-title: C/D-box snoRNAs form methylating and non-methylating ribonucleoprotein complexes: old dogs show new tricks publication-title: Bioessays doi: 10.1002/bies.201600264 – volume: 45 start-page: 1433 year: 2017 ident: 10.1016/j.isci.2018.11.007_bib16 article-title: High-throughput single-base resolution mapping of RNA 2-O-methylated residues publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkw810 – volume: 7 start-page: 219 year: 2012 ident: 10.1016/j.isci.2018.11.007_bib35 article-title: Molecular mechanisms of fragile X syndrome: a twenty-year perspective publication-title: Annu. Rev. Pathol. doi: 10.1146/annurev-pathol-011811-132457 – volume: 40 start-page: 560 year: 2015 ident: 10.1016/j.isci.2018.11.007_bib36 article-title: 'View from a Bridge': a new perspective on eukaryotic rRNA base modification publication-title: Trends Biochem. Sci. doi: 10.1016/j.tibs.2015.07.008 – volume: 289 start-page: 95 year: 2003 ident: 10.1016/j.isci.2018.11.007_bib2 article-title: NUFIP1 (nuclear FMRP interacting protein 1) is a nucleocytoplasmic shuttling protein associated with active synaptoneurosomes publication-title: Exp. Cell Res. doi: 10.1016/S0014-4827(03)00222-2 – volume: 383 start-page: 732 year: 1996 ident: 10.1016/j.isci.2018.11.007_bib6 article-title: Targeted ribose methylation of RNA in vivo directed by tailored antisense RNA guides publication-title: Nature doi: 10.1038/383732a0 – volume: 15 start-page: 1233 year: 2009 ident: 10.1016/j.isci.2018.11.007_bib42 article-title: Small RNAs derived from snoRNAs publication-title: RNA doi: 10.1261/rna.1528909 – volume: 15 start-page: 5408 year: 1996 ident: 10.1016/j.isci.2018.11.007_bib14 article-title: A nuclear role for the Fragile X mental retardation protein publication-title: EMBO J. doi: 10.1002/j.1460-2075.1996.tb00924.x – volume: 32 start-page: 1724 year: 2014 ident: 10.1016/j.isci.2018.11.007_bib24 article-title: Concise review: fragile X proteins in stem cell maintenance and differentiation publication-title: Stem Cells doi: 10.1002/stem.1698 – volume: 60 start-page: 201 year: 2008 ident: 10.1016/j.isci.2018.11.007_bib3 article-title: Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function publication-title: Neuron doi: 10.1016/j.neuron.2008.10.004 – volume: 39 start-page: 675 year: 2011 ident: 10.1016/j.isci.2018.11.007_bib5 article-title: Human box C/D snoRNAs with miRNA like functions: expanding the range of regulatory RNAs publication-title: Nucleic Acids Res. doi: 10.1093/nar/gkq776 – volume: 22 start-page: 1185 year: 2014 ident: 10.1016/j.isci.2018.11.007_bib31 article-title: Fragile X syndrome due to a missense mutation publication-title: Eur. J. Hum. Genet. doi: 10.1038/ejhg.2013.311 – volume: 12 start-page: 91 year: 1996 ident: 10.1016/j.isci.2018.11.007_bib18 article-title: The fragile X mental retardation protein is associated with ribosomes publication-title: Nat. Genet. doi: 10.1038/ng0196-91 – volume: 374 start-page: 32 year: 2013 ident: 10.1016/j.isci.2018.11.007_bib44 article-title: Neural differentiation of fragile X human embryonic stem cells reveals abnormal patterns of development despite successful neurogenesis publication-title: Dev. Biol. doi: 10.1016/j.ydbio.2012.11.031 – volume: 81 start-page: 941 year: 2016 ident: 10.1016/j.isci.2018.11.007_bib39 article-title: Nucleolar methyltransferase fibrillarin: evolution of structure and functions publication-title: Biochemistry (Mosc) doi: 10.1134/S0006297916090030 – volume: 9 start-page: e91465 year: 2014 ident: 10.1016/j.isci.2018.11.007_bib43 article-title: Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin publication-title: PLoS One doi: 10.1371/journal.pone.0091465 – volume: 22 start-page: 11 year: 2015 ident: 10.1016/j.isci.2018.11.007_bib22 article-title: Noncoding RNAs in eukaryotic ribosome biogenesis and function publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.2939 – volume: 42 start-page: 673 year: 2011 ident: 10.1016/j.isci.2018.11.007_bib30 article-title: Reversible inhibition of PSD-95 mRNA translation by miR-125a, FMRP phosphorylation, and mGluR signaling publication-title: Mol. Cell doi: 10.1016/j.molcel.2011.05.006 – volume: 67 start-page: 71 year: 2017 ident: 10.1016/j.isci.2018.11.007_bib38 article-title: Heterogeneous ribosomes preferentially translate distinct subpools of mRNAs genome-wide publication-title: Mol. Cell doi: 10.1016/j.molcel.2017.05.021 – volume: 1455 start-page: 249 year: 2016 ident: 10.1016/j.isci.2018.11.007_bib4 article-title: Quantitative proteomic analysis of the human nucleolus publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-3792-9_20 – volume: 16 start-page: 595 year: 2015 ident: 10.1016/j.isci.2018.11.007_bib33 article-title: Dysregulation and restoration of translational homeostasis in fragile X syndrome publication-title: Nat. Rev. Neurosci. doi: 10.1038/nrn4001 – volume: 17 start-page: 1539 year: 1997 ident: 10.1016/j.isci.2018.11.007_bib13 article-title: Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes publication-title: J. Neurosci. doi: 10.1523/JNEUROSCI.17-05-01539.1997 – volume: 1562 start-page: 171 year: 2017 ident: 10.1016/j.isci.2018.11.007_bib27 article-title: High-throughput mapping of 2'-O-Me residues in RNA using next-generation sequencing (illumina RiboMethSeq protocol) publication-title: Methods Mol. Biol. doi: 10.1007/978-1-4939-6807-7_12 – reference: 30763793 - iScience. 2019 Feb 11;12:368 |
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Snippet | FMRP is an RNA-binding protein that is known to localize in the cytoplasm and in the nucleus. Here, we have identified an interaction of FMRP with a specific... |
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Title | FMRP Interacts with C/D Box snoRNA in the Nucleus and Regulates Ribosomal RNA Methylation |
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