Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Gabrielle Bourgeois
- Michel Ney
- Imre Gaspar
- Christelle Aigueperse
- Matthias Schaefer
- Stefanie Kellner
- Mark Helm
- Yuri Motorin
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000358547600085&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1371/journal.pone.0133321
- Externe Identifier
- Clarivate Analytics Document Solution ID: CN6LZ
- PubMed Identifier: 26196125
- ISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- PLOS ONE
- Artikelnummer
- ARTN e0133321
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Titel
- Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120
- Sub types
- Article
- Ausgabe der Zeitschrift
- 10
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Gabrielle Bourgeois
- Michel Ney
- Imre Gaspar
- Christelle Aigueperse
- Matthias Schaefer
- Stefanie Kellner
- Mark Helm
- Yuri Motorin
- DOI
- 10.1371/journal.pone.0133321
- Editoren
- Thomas Preiss
- eISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- PLOS ONE
- Sprache
- en
- Online publication date
- 2015
- Paginierung
- e0133321 - e0133321
- Status
- Published online
- Herausgeber
- Public Library of Science (PLoS)
- Herausgeber URL
- http://dx.doi.org/10.1371/journal.pone.0133321
- Datum der Datenerfassung
- 2022
- Titel
- Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120
- Ausgabe der Zeitschrift
- 10
Datenquelle: Crossref
- Abstract
- Modified nucleotide 5-methylcytosine (m5C) is frequently present in various eukaryotic RNAs, including tRNAs, rRNAs and in other non-coding RNAs, as well as in mRNAs. RNA:m5C-methyltranferases (MTases) Nop2 from S. cerevisiae and human proliferation-associated nucleolar antigen p120 are both members of a protein family called Nop2/NSUN/NOL1. Protein p120 is well-known as a tumor marker which is over-expressed in various cancer tissues. Using a combination of RNA bisulfite sequencing and HPLC-MS/MS analysis, we demonstrated here that p120 displays an RNA:m5C- MTase activity, which restores m5C formation at position 2870 in domain V of 25S rRNA in a nop2Δ yeast strain. We also confirm that yeast proteins Nop2p and Rcm1p catalyze the formation of m5C in domains V and IV, respectively. In addition, we do not find any evidence of m5C residues in yeast 18S rRNA. We also performed functional complementation of Nop2-deficient yeasts by human p120 and studied the importance of different sequence and structural domains of Nop2 and p120 for yeast growth and m5C-MTase activity. Chimeric protein formed by Nop2 and p120 fragments revealed the importance of Nop2 N-terminal domain for correct protein localization and its cellular function. We also validated that the presence of Nop2, rather than the m5C modification in rRNA itself, is required for pre-rRNA processing. Our results corroborate that Nop2 belongs to the large family of pre-ribosomal proteins and possesses two related functions in pre-rRNA processing: as an essential factor for cleavages and m5C:RNA:modification. These results support the notion of quality control during ribosome synthesis by such modification enzymes.
- Addresses
- Laboratoire IMoPA, UMR 7365 UL-CNRS, BioPole de UL, Vandoeuvre-les-Nancy, France.
- Autoren
- Gabrielle Bourgeois
- Michel Ney
- Imre Gaspar
- Christelle Aigueperse
- Matthias Schaefer
- Stefanie Kellner
- Mark Helm
- Yuri Motorin
- DOI
- 10.1371/journal.pone.0133321
- eISSN
- 1932-6203
- Externe Identifier
- PubMed Identifier: 26196125
- PubMed Central ID: PMC4510066
- Open access
- true
- ISSN
- 1932-6203
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- PloS one
- Schlüsselwörter
- Humans
- Saccharomyces cerevisiae
- 5-Methylcytosine
- Methyltransferases
- tRNA Methyltransferases
- Saccharomyces cerevisiae Proteins
- Nuclear Proteins
- RNA, Ribosomal
- Protein Structure, Tertiary
- Protein Binding
- Sprache
- eng
- Medium
- Electronic-eCollection
- Online publication date
- 2015
- Open access status
- Open Access
- Paginierung
- e0133321
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2015
- Titel
- Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 10
Datenquelle: Europe PubMed Central
- Abstract
- Modified nucleotide 5-methylcytosine (m5C) is frequently present in various eukaryotic RNAs, including tRNAs, rRNAs and in other non-coding RNAs, as well as in mRNAs. RNA:m5C-methyltranferases (MTases) Nop2 from S. cerevisiae and human proliferation-associated nucleolar antigen p120 are both members of a protein family called Nop2/NSUN/NOL1. Protein p120 is well-known as a tumor marker which is over-expressed in various cancer tissues. Using a combination of RNA bisulfite sequencing and HPLC-MS/MS analysis, we demonstrated here that p120 displays an RNA:m5C- MTase activity, which restores m5C formation at position 2870 in domain V of 25S rRNA in a nop2Δ yeast strain. We also confirm that yeast proteins Nop2p and Rcm1p catalyze the formation of m5C in domains V and IV, respectively. In addition, we do not find any evidence of m5C residues in yeast 18S rRNA. We also performed functional complementation of Nop2-deficient yeasts by human p120 and studied the importance of different sequence and structural domains of Nop2 and p120 for yeast growth and m5C-MTase activity. Chimeric protein formed by Nop2 and p120 fragments revealed the importance of Nop2 N-terminal domain for correct protein localization and its cellular function. We also validated that the presence of Nop2, rather than the m5C modification in rRNA itself, is required for pre-rRNA processing. Our results corroborate that Nop2 belongs to the large family of pre-ribosomal proteins and possesses two related functions in pre-rRNA processing: as an essential factor for cleavages and m5C:RNA:modification. These results support the notion of quality control during ribosome synthesis by such modification enzymes.
- Date of acceptance
- 2015
- Autoren
- Gabrielle Bourgeois
- Michel Ney
- Imre Gaspar
- Christelle Aigueperse
- Matthias Schaefer
- Stefanie Kellner
- Mark Helm
- Yuri Motorin
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/26196125
- DOI
- 10.1371/journal.pone.0133321
- eISSN
- 1932-6203
- Externe Identifier
- PubMed Central ID: PMC4510066
- Ausgabe der Veröffentlichung
- 7
- Zeitschrift
- PLoS One
- Schlüsselwörter
- 5-Methylcytosine
- Humans
- Methyltransferases
- Nuclear Proteins
- Protein Binding
- Protein Structure, Tertiary
- RNA, Ribosomal
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- tRNA Methyltransferases
- Sprache
- eng
- Country
- United States
- Paginierung
- e0133321
- PII
- PONE-D-15-13122
- Datum der Veröffentlichung
- 2015
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2016
- Titel
- Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 10
Datenquelle: PubMed
- Beziehungen:
- Eigentum von