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
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
2008
Dolichyl-Phosphate-Glucose Is Used To Make O-Glycans on Glycoproteins of Trichomonas vaginalis▿ †
Grabińska K, Ghosh S, Guan Z, Cui J, Raetz C, Robbins P, Samuelson J. Dolichyl-Phosphate-Glucose Is Used To Make O-Glycans on Glycoproteins of Trichomonas vaginalis▿ †. MSphere 2008, 7: 1344-1351. PMID: 18552282, PMCID: PMC2519777, DOI: 10.1128/ec.00061-08.Peer-Reviewed Original ResearchConceptsDol-P-Man synthase activityO-glycansSynthase activityNumerous gene duplicationsSaccharomyces cerevisiae membranesDolichyl-P-mannose synthaseN-glycosylation defectGene duplicationHuge genomeDPM1 geneNumerous genesGlycosylation defectsDolichyl-PPGene productsRecombinant proteinsSugar donorIsoprene unitsEndogenous glycoproteinsGenesDolichyl phosphateMembraneGlycoproteinFirst demonstrationProtistsALG5
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 ResearchConceptsEnzymatic activityCis-prenyltransferase activityLong-chain dolicholsYeast SaccharomycesShorter speciesRER2Dolichol biosynthesisLevels of mRNADiphosphate formationIsoprene unitsSRT1SaccharomycesOverexpressionDolichol contentGenesPreferential synthesisProteinFunctional relationshipMRNADPM1TranscriptionBiosynthesisFarnesylSpecies