A New Nuclear Function of the Entamoeba histolytica Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Activity
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Ayala Tovy
- Rama Siman Tov
- Ricarda Gaentzsch
- Mark Helm
- Serge Ankri
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000275295900025&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1371/journal.ppat.1000775
- eISSN
- 1553-7374
- Externe Identifier
- Clarivate Analytics Document Solution ID: 565LZ
- PubMed Identifier: 20174608
- ISSN
- 1553-7366
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PLOS PATHOGENS
- Artikelnummer
- ARTN e1000775
- Datum der Veröffentlichung
- 2010
- Status
- Published
- Titel
- A New Nuclear Function of the <i>Entamoeba histolytica</i> Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Activity
- Sub types
- Article
- Ausgabe der Zeitschrift
- 6
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Ayala Tovy
- Rama Siman Tov
- Ricarda Gaentzsch
- Mark Helm
- Serge Ankri
- DOI
- 10.1371/journal.ppat.1000775
- Editoren
- William A Petri
- eISSN
- 1553-7374
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PLoS Pathogens
- Sprache
- en
- Online publication date
- 2010
- Paginierung
- e1000775 - e1000775
- Status
- Published online
- Herausgeber
- Public Library of Science (PLoS)
- Herausgeber URL
- http://dx.doi.org/10.1371/journal.ppat.1000775
- Datum der Datenerfassung
- 2021
- Titel
- A New Nuclear Function of the Entamoeba histolytica Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Activity
- Ausgabe der Zeitschrift
- 6
Datenquelle: Crossref
- Abstract
- Cytosine-5 methyltransferases of the Dnmt2 family function as DNA and tRNA methyltransferases. Insight into the role and biological significance of Dnmt2 is greatly hampered by a lack of knowledge about its protein interactions. In this report, we address the subject of protein interaction by identifying enolase through a yeast two-hybrid screen as a Dnmt2-binding protein. Enolase, which is known to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), was shown to have both a cytoplasmatic and a nuclear localization in the parasite Entamoeba histolytica. We discovered that enolase acts as a Dnmt2 inhibitor. This unexpected inhibitory activity was antagonized by 2-PG, which suggests that glucose metabolism controls the non-glycolytic function of enolase. Interestingly, glucose starvation drives enolase to accumulate within the nucleus, which in turn leads to the formation of additional enolase-E.histolytica DNMT2 homolog (Ehmeth) complex, and to a significant reduction of the tRNA(Asp) methylation in the parasite. The crucial role of enolase as a Dnmt2 inhibitor was also demonstrated in E.histolytica expressing a nuclear localization signal (NLS)-fused-enolase. These results establish enolase as the first Dnmt2 interacting protein, and highlight an unexpected role of a glycolytic enzyme in the modulation of Dnmt2 activity.
- Addresses
- Department of Molecular Microbiology, The Bruce Rappaport Faculty of Medicine, Technion, Haifa, Israel.
- Autoren
- Ayala Tovy
- Rama Siman Tov
- Ricarda Gaentzsch
- Mark Helm
- Serge Ankri
- DOI
- 10.1371/journal.ppat.1000775
- eISSN
- 1553-7374
- Externe Identifier
- PubMed Identifier: 20174608
- PubMed Central ID: PMC2824750
- Open access
- true
- ISSN
- 1553-7366
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PLoS pathogens
- Schlüsselwörter
- Cell Nucleus
- Entamoeba histolytica
- Phosphopyruvate Hydratase
- Protozoan Proteins
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Two-Hybrid System Techniques
- Polymerase Chain Reaction
- Immunoprecipitation
- DNA (Cytosine-5-)-Methyltransferases
- Sprache
- eng
- Medium
- Electronic
- Online publication date
- 2010
- Open access status
- Open Access
- Paginierung
- e1000775
- Datum der Veröffentlichung
- 2010
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2010
- Titel
- A new nuclear function of the Entamoeba histolytica glycolytic enzyme enolase: the metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2) activity.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 6
Files
https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000775&type=printable https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20174608/pdf/?tool=EBI https://europepmc.org/articles/PMC2824750?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- Cytosine-5 methyltransferases of the Dnmt2 family function as DNA and tRNA methyltransferases. Insight into the role and biological significance of Dnmt2 is greatly hampered by a lack of knowledge about its protein interactions. In this report, we address the subject of protein interaction by identifying enolase through a yeast two-hybrid screen as a Dnmt2-binding protein. Enolase, which is known to catalyze the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), was shown to have both a cytoplasmatic and a nuclear localization in the parasite Entamoeba histolytica. We discovered that enolase acts as a Dnmt2 inhibitor. This unexpected inhibitory activity was antagonized by 2-PG, which suggests that glucose metabolism controls the non-glycolytic function of enolase. Interestingly, glucose starvation drives enolase to accumulate within the nucleus, which in turn leads to the formation of additional enolase-E.histolytica DNMT2 homolog (Ehmeth) complex, and to a significant reduction of the tRNA(Asp) methylation in the parasite. The crucial role of enolase as a Dnmt2 inhibitor was also demonstrated in E.histolytica expressing a nuclear localization signal (NLS)-fused-enolase. These results establish enolase as the first Dnmt2 interacting protein, and highlight an unexpected role of a glycolytic enzyme in the modulation of Dnmt2 activity.
- Date of acceptance
- 2010
- Autoren
- Ayala Tovy
- Rama Siman Tov
- Ricarda Gaentzsch
- Mark Helm
- Serge Ankri
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/20174608
- DOI
- 10.1371/journal.ppat.1000775
- eISSN
- 1553-7374
- Externe Identifier
- PubMed Central ID: PMC2824750
- Ausgabe der Veröffentlichung
- 2
- Zeitschrift
- PLoS Pathog
- Schlüsselwörter
- Cell Nucleus
- DNA (Cytosine-5-)-Methyltransferases
- Entamoeba histolytica
- Immunoprecipitation
- Phosphopyruvate Hydratase
- Polymerase Chain Reaction
- Protozoan Proteins
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Two-Hybrid System Techniques
- Sprache
- eng
- Country
- United States
- Paginierung
- e1000775
- Datum der Veröffentlichung
- 2010
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2010
- Titel
- A new nuclear function of the Entamoeba histolytica glycolytic enzyme enolase: the metabolic regulation of cytosine-5 methyltransferase 2 (Dnmt2) activity.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 6
Datenquelle: PubMed
- Beziehungen:
- Eigentum von