2020
Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation
Edani BH, Grabińska KA, Zhang R, Park EJ, Siciliano B, Surmacz L, Ha Y, Sessa WC. Structural elucidation of the cis-prenyltransferase NgBR/DHDDS complex reveals insights in regulation of protein glycosylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 20794-20802. PMID: 32817466, PMCID: PMC7456142, DOI: 10.1073/pnas.2008381117.Peer-Reviewed Original ResearchConceptsActive site tunnelProtein glycosylationAtomic resolution structuresGlycosyl carrier lipidsΑ3 helixEnzyme active sitePTase activityResolution structureActive siteEndoplasmic reticulumHomodimeric formCarrier lipidRate-limiting stepGlycosylationCrystal structureDHDDSStructural elucidationPTaseIsoprene chainPrenyltransferaseUnique insightsComplexesUnfavorable stateNgBRHomodimeric
2017
A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity
Grabińska KA, Edani BH, Park EJ, Kraehling JR, Sessa WC. A conserved C-terminal RXG motif in the NgBR subunit of cis-prenyltransferase is critical for prenyltransferase activity. Journal Of Biological Chemistry 2017, 292: 17351-17361. PMID: 28842490, PMCID: PMC5655512, DOI: 10.1074/jbc.m117.806034.Peer-Reviewed Original ResearchConceptsUndecaprenyl diphosphate synthaseDiphosphate synthaseDomains of lifeProtein glycosylation reactionsStrong conservationCellular functionsG motifTerminal tailPrenyltransferase activityFirst enzymeCis-prenyltransferaseBacterial enzymesIsoprene unitsSubunitsLarge familyNgBREnzyme activityG sequencesEnzymeDolichyl phosphateMotifSynthaseEukaryotesOrthologsArchaea
2014
Mutation of Nogo-B Receptor, a Subunit of cis-Prenyltransferase, Causes a Congenital Disorder of Glycosylation
Park EJ, Grabińska K, Guan Z, Stránecký V, Hartmannová H, Hodaňová K, Barešová V, Sovová J, Jozsef L, Ondrušková N, Hansíková H, Honzík T, Zeman J, Hůlková H, Wen R, Kmoch S, Sessa WC. Mutation of Nogo-B Receptor, a Subunit of cis-Prenyltransferase, Causes a Congenital Disorder of Glycosylation. Cell Metabolism 2014, 20: 448-457. PMID: 25066056, PMCID: PMC4161961, DOI: 10.1016/j.cmet.2014.06.016.Peer-Reviewed Original ResearchConceptsProtein glycosylationCis-prenyltransferaseGPI anchor biosynthesisDolichol synthesisSynthesis of dolicholO-mannosylationAnchor biosynthesisFirst enzymeGenetic basisC-terminusCongenital disorderFunction mutationsGlycosylationEssential roleEnhanced accumulationMutationsYeastNgBRSubunitsDolicholFibroblastsBiosynthesisTerminusFree cholesterolProtein
2010
Molecular characterization of the cis-prenyltransferase of Giardia lamblia
Grabińska K, Cui J, Chatterjee A, Guan Z, Raetz C, Robbins P, Samuelson J. Molecular characterization of the cis-prenyltransferase of Giardia lamblia. Glycobiology 2010, 20: 824-832. PMID: 20308470, PMCID: PMC2900897, DOI: 10.1093/glycob/cwq036.Peer-Reviewed Original ResearchConceptsIsoprene unitsDouble deletion mutantGPI anchor synthesisMost eukaryotesHigher eukaryotesAnchor synthesisN-glycosylationGlycosylphosphatidylinositol (GPI) anchorCis-prenyltransferaseKinase activityPolyprenyl pyrophosphateBacterial enzymesDolichol kinase activityDolichol kinaseMolecular characterizationImportant enzymeN-glycansEukaryotesProtistsPolyprenol lipidsNormal growthPyrophosphate linkageEnzymeGiardia lambliaDolichol
2009
The YTA7 gene is involved in the regulation of the isoprenoid pathway in the yeast Saccharomyces cerevisiae
Kuranda K, Grabinska K, Berges T, Karst F, Leberre V, Sokol S, François J, Palamarczyk G. The YTA7 gene is involved in the regulation of the isoprenoid pathway in the yeast Saccharomyces cerevisiae. FEMS Yeast Research 2009, 9: 381-390. PMID: 19416104, DOI: 10.1111/j.1567-1364.2009.00485.x.Peer-Reviewed Original ResearchConceptsIsoprenoid pathwayFPP synthaseTwo-hybrid screenMembrane-associated proteinsBiosynthesis of hemeIsoprenoid biosynthesisProtein partnersPresence of lovastatinYeast SaccharomycesN-glycosylationSterol biosynthesisSqualene synthaseCis-prenyltransferaseEndoplasmic reticulumIsoprenoid compoundsZaragozic acidsBiosynthesisCellular levelGenesEnzymatic activityExpression levelsSaccharomycesPathwaySynthaseRegulation
2005
Functional relationships between the Saccharomyces cerevisiae cis-prenyltransferases required for dolichol biosynthesis.
Grabińska K, Sosińska G, Orłowski J, Swiezewska E, Berges T, Karst F, Palamarczyk G. Functional relationships between the Saccharomyces cerevisiae cis-prenyltransferases required for dolichol biosynthesis. Acta Biochimica Polonica 2005, 52: 221-32. PMID: 15827619, DOI: 10.18388/abp.2005_3511.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceDNA PrimersDolicholsGenes, FungalSaccharomyces cerevisiaeTranscription, GeneticTransferasesConceptsEnzymatic activityCis-prenyltransferase activityLong-chain dolicholsYeast SaccharomycesShorter speciesRER2Dolichol biosynthesisLevels of mRNADiphosphate formationIsoprene unitsSRT1SaccharomycesOverexpressionDolichol contentGenesPreferential synthesisProteinFunctional relationshipMRNADPM1TranscriptionBiosynthesisFarnesylSpecies
1997
Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression
Szkopińska A, Grabińska K, Delourme D, Karst F, Rytka J, Palamarczyk G. Polyprenol formation in the yeast Saccharomyces cerevisiae: effect of farnesyl diphosphate synthase overexpression. Journal Of Lipid Research 1997, 38: 962-968. PMID: 9186913, DOI: 10.1016/s0022-2275(20)37220-5.Peer-Reviewed Original ResearchConceptsWild-type yeastType yeastSaccharomyces cerevisiaeYeast Saccharomyces cerevisiaeEffects of farnesylSynthesis of dolicholSame genetic backgroundHand overexpressionErg mutantsFPP synthaseSqualene synthase activitySynthesis of polyprenolsExogenous FPPMevalonate pathwayMutantsGenetic backgroundYeastOverexpressionSynthase overexpressionSynthase activityCerevisiaeFarnesylGenesSynthasePolyprenols