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 iniScience Vol. 9; pp. 399 - 411
Main Authors D'Souza, Michelle Ninochka, Gowda, Naveen Kumar Chandappa, Tiwari, Vishal, Babu, Rosana Ottakandathil, Anand, Praveen, Dastidar, Sudhriti Ghosh, Singh, Randhir, James, Owen G., Selvaraj, Bhuvaneish, Pal, Rakhi, Ramesh, Arati, Chattarji, Sumantra, Chandran, Siddharthan, Gulyani, Akash, Palakodeti, Dasaradhi, Muddashetty, Ravi S.
Format Journal Article
LanguageEnglish
Published United States Elsevier 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.
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
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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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Keywords Molecular Interaction
Stem Cells Research
Omics
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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
URI https://www.ncbi.nlm.nih.gov/pubmed/30469012
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