0000000001020848

AUTHOR

Ricarda Gaentzsch

showing 1 related works from this author

A New Nuclear Function of the Entamoeba histolytica Glycolytic Enzyme Enolase: The Metabolic Regulation of Cytosine-5 Methyltransferase 2 (Dnmt2) Act…

2009

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…

MethyltransferaseQH301-705.5ImmunologyEnolaseProtozoan ProteinsPolymerase Chain ReactionMicrobiologyEntamoeba histolyticaTwo-Hybrid System TechniquesGenetics and Genomics/EpigeneticsVirologyGeneticsImmunoprecipitationDNA (Cytosine-5-)-MethyltransferasesMicrobiology/ParasitologyBiology (General)Molecular BiologyMolecular Biology/DNA MethylationCell Nucleuschemistry.chemical_classificationbiologyEntamoeba histolyticaInfectious Diseases/Protozoal InfectionsMethylationRC581-607biology.organism_classificationTRNA MethyltransferasesEnolase 2EnzymechemistryBiochemistryPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationParasitologyImmunologic diseases. AllergyNuclear localization sequenceResearch ArticlePLoS Pathogens
researchProduct