Search results for "Intramolecular Transferases"

showing 3 items of 3 documents

β-Amyrin Synthase1 Controls the Accumulation of the Major Saponins Present in Pea (Pisum sativum)

2021

Abstract The use of pulses as ingredients for the production of food products rich in plant proteins is increasing. However, protein fractions prepared from pea or other pulses contain significant amounts of saponins, glycosylated triterpenes that can impart an undesirable bitter taste when used as an ingredient in foodstuffs. In this article, we describe the identification and characterization of a gene involved in saponin biosynthesis during pea seed development, by screening mutants obtained from two Pisum sativum TILLING (Targeting Induced Local Lesions IN Genomes) populations in two different genetic backgrounds. The mutations studied are located in a gene designated PsBAS1 (β-amyrin s…

0106 biological sciencesTILLINGPhysiologyMutantNonsense mutationPlant Sciencemedicine.disease_cause01 natural sciencesPisum03 medical and health sciencesSpatio-Temporal AnalysisSativumGene Expression Regulation PlantLoss of Function Mutationmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyIntramolecular TransferasesGenePlant Proteins030304 developmental biology2. Zero hunger[SDV.EE]Life Sciences [q-bio]/Ecology environment0303 health sciencesMutationbiologyPeasfood and beveragesCell BiologyGeneral MedicineSaponinsbiology.organism_classificationBiochemistrySeedsFunctional genomics010606 plant biology & botany
researchProduct

Biallelic pathogenic variants in the lanosterol synthase gene LSS involved in the cholesterol biosynthesis cause alopecia with intellectual disabilit…

2019

International audience; Purpose Lanosterol synthase (LSS) gene was initially described in families with extensive congenital cataracts. Recently, a study has highlighted LSS associated with hypotrichosis simplex. We expanded the phenotypic spectrum of LSS to a recessive neuroectodermal syndrome formerly named alopecia with mental retardation (APMR) syndrome. It is a rare autosomal recessive condition characterized by hypotrichosis and intellectual disability (ID) or developmental delay (DD), frequently associated with early-onset epilepsy and other dermatological features. Methods Through a multicenter international collaborative study, we identified LSS pathogenic variants in APMR individu…

MaleDevelopmental DisabilitiesIntellectual disabilitycholesterol pathwayWhole Exome Sequencingchemistry.chemical_compoundMissense mutationAge of OnsetChildIntramolecular TransferasesGenetics (clinical)Exome sequencingGeneticsSanger sequencing0303 health sciencesbiologyLanosterol030305 genetics & heredityLSS3. Good healthPedigreeCholesterolPhenotypeintellectual disabilityChild PreschoolAllelic ImbalanceCongenital cataractssymbolsFemaleSqualeneearly-onset epileptic encephalopathy03 medical and health sciencessymbols.namesakeLanosterolCholesterol pathwayExome SequencingmedicineHumans030304 developmental biologyEpilepsyInfantAlopeciaalopeciamedicine.diseaseEarly-onset epileptic encephalopathychemistryMutationbiology.proteinHypotrichosis[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology[SDV.MHEP.DERM]Life Sciences [q-bio]/Human health and pathology/DermatologyLanosterol synthase
researchProduct

Pseudouridine: Still mysterious, but never a fake (uridine)!

2014

International audience; Pseudouridine () is the most abundant of >150 nucleoside modifications in RNA. Although was discovered as the first modified nucleoside more than half a century ago, neither the enzymatic mechanism of its formation, nor the function of this modification are fully elucidated. We present the consistent picture of synthases, their substrates and their substrate positions in model organisms of all domains of life as it has emerged to date and point out the challenges that remain concerning higher eukaryotes and the elucidation of the enzymatic mechanism.

RNA MitochondrialSaccharomyces cerevisiaeReviewBiologyModified nucleosidesPseudouridine03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA modificationEscherichia coliHumansRNA Processing Post-Transcriptional[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Intramolecular TransferasesUridineMolecular Biology030304 developmental biology0303 health sciencesRNACell BiologyRNA Transfer Amino Acid-SpecificRibonucleoproteins Small NuclearUridineIsoenzymeschemistryBiochemistryRNA Ribosomal030220 oncology & carcinogenesisTransfer RNANucleic Acid ConformationRNARibosomesNucleosidePseudouridineSmall nuclear RNA[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyRNA Guide Kinetoplastida
researchProduct