Search results for "Multienzyme Complexes"

showing 10 items of 50 documents

Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: towards the characterization of "plant defense prote…

2003

Plants have evolved efficient mechanisms to resist pathogens. The earliest defense response is the hypersensitive response (HR) considered as the main step leading to plant systemic acquired resistance (SAR) that protects the whole plant against a large spectrum of pathogens. We showed previously that elicitation of defense reactions in tobacco cells by cryptogein, a proteinaceous elicitor of plant defense reactions, leads to a rapid and differential accumulation of transcripts corresponding to genes encoding defense-induced (din) subunits of 20S proteasome: beta1din, alpha3din and alpha6din.Here, expression of these three subunits was investigated by Northern blotting and by Western blotti…

0106 biological sciencesHypersensitive responseProteasome Endopeptidase Complex[SDV]Life Sciences [q-bio]Protein subunitBlotting WesternGene ExpressionBiology01 natural sciencesBiochemistryMixed Function OxygenasesFungal Proteins03 medical and health sciencesMultienzyme ComplexesTobaccoPlant defense against herbivoryElectrophoresis Gel Two-DimensionalNorthern blotComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesAlgal ProteinsProteinsCell BiologyBlotting NorthernMolecular biologyCell biologyElicitor[SDV] Life Sciences [q-bio]BlotPlant LeavesTobacco Mosaic VirusCysteine EndopeptidasesProteasomeEnzyme InductionREPONSE DE LA PLANTESystemic acquired resistance010606 plant biology & botanyPeptide HydrolasesThe international journal of biochemistrycell biology
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Analysis of substrate binding in individual active sites of bifunctional human ATIC

2018

Aminoimidazolecarboxamide ribonucleotide formyl transferase (AICARFT): Inosine monophosphate cyclohydrolase (IMPCH, collectively called ATIC) is a bifunctional enzyme that catalyses the penultimate and final steps in the purine de novo biosynthesis pathway. The bifunctional protein is dimeric and each monomer contains two different active sites both of which are capable of binding nucleotide substrates, this means to a potential total of four distinct binding events might be observed. Within this work we used a combination of site-directed and truncation mutants of ATIC to independently investigate the binding at these two sites using calorimetry. A single S10W mutation is sufficient to blo…

0301 basic medicineHydroxymethyl and Formyl TransferasesModels MolecularRibonucleotideStereochemistryBiophysicsBiochemistryAnalytical ChemistrySubstrate Specificity03 medical and health scienceschemistry.chemical_compoundMultienzyme ComplexesCatalytic DomainTransferaseHumansNucleotidePhosphofructokinase 2Bifunctional enzymesMolecular Biologychemistry.chemical_classification030102 biochemistry & molecular biologybiologyNucleotidesActive siteCooperative bindingIsothermal titration calorimetryXanthosine monophosphate030104 developmental biologyBiochemistrychemistryNucleotide DeaminasesMultiple binding sitesbiology.proteinIsothermal titration calorimetryProtein Binding
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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

2020

13 páginas, 6 figuras, 3 tablas

0301 basic medicineModels MolecularBioquímicaHistidine KinaseProtein ConformationScience030106 microbiologyPhosphataseGeneral Physics and AstronomyMicrobiologiaCrystallography X-RayModels BiologicalBiochemistryMicrobiologyGeneral Biochemistry Genetics and Molecular BiologyCatalysisArticleEnzyme catalysis03 medical and health sciencesResidue (chemistry)Protein structureBacterial ProteinsMultienzyme ComplexesHistidineThermotoga maritimaPhosphorylationlcsh:ScienceAuthor CorrectionHistidineX-ray crystallographyMultidisciplinaryEffectorChemistryEscherichia coli ProteinsQGeneral ChemistryHydrogen-Ion ConcentrationResponse regulator030104 developmental biologyBiochemistryMutationTrans-ActivatorsPhosphorylationlcsh:QBacterial Outer Membrane Proteins
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Genetic organization of the citCDEF locus and identification of mae and clyR genes from Leuconostoc mesenteroides.

1999

ABSTRACT In this paper, we describe two open reading frames coding for a NAD-dependent malic enzyme ( mae ) and a putative regulatory protein ( clyR ) found in the upstream region of citCDEFG of Leuconostoc mesenteroides subsp. cremoris 195. The transcriptional analysis of the citrate lyase locus revealed one polycistronic mRNA covering the mae and citCDEF genes. This transcript was detected only on RNA prepared from cells grown in the presence of citrate. Primer extension experiments suggest that clyR and the citrate lyase operon are expressed from a bidirectional A-T-rich promoter region located between mae and clyR.

ATP citrate lyaseTranscription GeneticOperonMolecular Sequence DataMalatesLocus (genetics)Genetics and Molecular BiologyBiologyMicrobiologyPrimer extensionCitric AcidOpen Reading FramesBacterial ProteinsMalate DehydrogenaseMultienzyme ComplexesLeuconostocAmino Acid SequenceMolecular BiologyGeneGeneticsBase SequenceOxo-Acid-LyasesPromoterGene Expression Regulation BacterialSequence Analysis DNAbiology.organism_classificationMolecular biologyLeuconostoc mesenteroidesGenes BacterialSequence AlignmentLeuconostocJournal of bacteriology
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Inhibitory effects on mitochondrial complex I of semisynthetic mono-Tetrahydrofuran acetogenin derivatives

2003

Modifications in the terminal alpha,beta-unsaturated gamma-methyl-gamma-lactone moiety or in the alkyl chain that links this terminal gamma-lactone with the alpha,alpha'-dihydroxylated THF system of the natural mono-tetrahydrofuranic acetogenins, annonacin and annonacinone, led to the preparation of eight semisynthetic derivatives. Their inhibitory effects on mitochondrial complex I is discussed and compared with that of the classical complex I inhibitor, rotenone.

AcetogeninsStereochemistryClinical BiochemistryRespiratory chainAnnonacinPharmaceutical ScienceBiochemistryChemical synthesisLactoneschemistry.chemical_compoundMultienzyme ComplexesDrug DiscoveryMoietyNADH NADPH OxidoreductasesEnzyme InhibitorsFuransMolecular BiologyTetrahydrofuranchemistry.chemical_classificationElectron Transport Complex IOrganic ChemistryRotenoneKineticschemistryAcetogeninMolecular MedicineFatty AlcoholsLactoneBioorganic & Medicinal Chemistry Letters
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Defects in the Human Leukocyte Antigen Class I Antigen Processing Machinery in Head and Neck Squamous Cell Carcinoma: Association with Clinical Outco…

2005

AbstractPurpose: Human leukocyte antigen (HLA) class I antigen defects, which are frequently present in head and neck squamous cell carcinoma (HNSCC) cells may provide the tumor with an escape mechanism from immune surveillance. Scanty information is available about mechanisms underlying HLA class I antigen defects in both lesions and cell lines from HNSCC. In this study, we investigate the role of antigen processing machinery (APM) component abnormalities in the generation of deficient HLA class I surface expression of HNSCC cells.Experimental Design: Using immunohistochemistry, Western blot, and RT-PCR analyses we correlated the expression of the IFN-γ inducible proteasome subunits and of…

AdultMaleProteasome Endopeptidase ComplexCancer ResearchPathologymedicine.medical_specialtyBlotting WesternDown-RegulationHuman leukocyte antigenBiologyCell LineInterferon-gammaATP Binding Cassette Transporter Subfamily B Member 3HLA AntigensMultienzyme ComplexesCell Line TumorTumor Cells Culturedotorhinolaryngologic diseasesmedicineCarcinomaHumansATP Binding Cassette Transporter Subfamily B Member 2AgedReverse Transcriptase Polymerase Chain ReactionAntigen processingHistocompatibility Antigens Class ICancerMiddle Agedmedicine.diseaseImmunohistochemistrySurvival AnalysisHead and neck squamous-cell carcinomaGene Expression Regulation NeoplasticCysteine Endopeptidasesstomatognathic diseasesOncologyHead and Neck NeoplasmsCarcinoma Squamous Cellbiology.proteinImmunohistochemistryTAP2ATP-Binding Cassette TransportersFemaleTAP1Clinical Cancer Research
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Association of microsatellite polymorphisms of the human 14q13.2 region with type 2 diabetes mellitus in Latvian and Finnish populations.

2007

A polymorphic microsatellite in intron 6 of the human proteasome core particle PSMA6 gene (HSMS006), and four other microsatellites localized upstream on human chromosome 14q13.2 (HSMS801, HSMS702, HSMS701, HSMS602), were genotyped in 104 type 2 diabetic patients and 129 age-matched control subjects from Latvia and replicated in 91 type 2 diabetic patients and 88 age-matched healthy control subjects from the Botnia Study in Finland. In type 2 diabetic patients from both populations the HSMS006 (TG)22 allele was two times more frequent compared to the control group. In the Latvian population the (CAA)8 allele of the HSMS602 marker was less frequent in the diabetic group, as was the (AC)24 al…

AdultMaleProteasome Endopeptidase ComplexPopulationPSMA6Type 2 diabetesBiologyGene FrequencyPolymorphism (computer science)Multienzyme ComplexesGeneticsmedicineHumansAlleleeducationAllele frequencyGenetics (clinical)AllelesFinlandAgedGeneticsChromosomes Human Pair 14education.field_of_studyPolymorphism GeneticType 2 Diabetes MellitusMiddle Agedmedicine.diseaseLatviaDiabetes Mellitus Type 2Case-Control StudiesMicrosatelliteFemaleMicrosatellite RepeatsAnnals of human genetics
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An essential switch in subunit composition of a chromatin remodeling complex during neural development.

2007

Summary Mammalian neural stem cells (NSCs) have the capacity to both self-renew and to generate all the neuronal and glial cell-types of the adult nervous system. Global chromatin changes accompany the transition from proliferating NSCs to committed neuronal lineages, but the mechanisms involved have been unclear. Using a proteomics approach, we show that a switch in subunit composition of neural, ATP-dependent SWI/SNF-like chromatin remodeling complexes accompanies this developmental transition. Proliferating neural stem and progenitor cells express complexes in which BAF45a, a Kruppel/PHD domain protein and the actin-related protein BAF53a are quantitatively associated with the SWI2/SNF2-…

Cellular differentiationProtein subunitNeuroscience(all)Molecular Sequence DataNeuroepithelial CellsDEVBIONerve Tissue ProteinsBiologyChromatin remodelingMOLNEUROEpigenesis Genetic03 medical and health sciencesMice0302 clinical medicineMultienzyme ComplexesAnimalsAmino Acid SequenceProgenitor cell030304 developmental biologyNeurons0303 health sciencesGeneral NeuroscienceMultipotent Stem CellsGene Expression Regulation DevelopmentalCell DifferentiationChromatin Assembly and DisassemblySTEMCELLNeural stem cellChromatinCell biologyNeuroepithelial cellProtein SubunitsNeural developmentNeuroglia030217 neurology & neurosurgeryTranscription FactorsNeuron
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The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking pept…

1998

A high proportion of tumors arise due to mutation of the p53 tumor suppressor protein. A p53 hotspot mutation at amino acid position 273 from R to H, flanking a peptide epitope that spans residues 264–272, renders cells resistant to killing by human histocompatibility leukocyte antigen (HLA)-A*0201–restricted cytotoxic T lymphocytes (CTLs) specific for this epitope. Acquisition of the R to H mutation at residue 273 of the human p53 protein promotes tumor growth in vivo by selective escape from recognition by p53.264–272 peptide-specific CTLs. Synthetic 27-mer p53 polypeptides covering the antigenic nonamer region 264–272 of p53 were used as proteasome substrates to investigate whether the R…

Cytotoxicity Immunologicp53Epitopes T-LymphocyteEpitopeSubstrate SpecificityMice0302 clinical medicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellPeptide sequence0303 health sciencesAntigen PresentationproteasomesHydrolysisArticles3. Good healthCysteine Endopeptidasestumor antigensCell DivisionProteasome Endopeptidase ComplexImmunologyAntigen presentationMolecular Sequence DataMice TransgenicBiologyArgininecytotoxic T lymphocytes03 medical and health sciencesAntigenMultienzyme Complexesantigen processingAnimalsHumansPoint MutationHistidineAmino Acid Sequence030304 developmental biologyBinding SitesLinear epitopeHLA-A AntigensPoint mutationCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCTL*Tumor Suppressor Protein p53Peptides030215 immunologyT-Lymphocytes CytotoxicThe Journal of experimental medicine
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Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster

1998

ABSTRACT A citrate lyase (EC 4.1.3.6 ) was purified 25-fold from Leuconostoc mesenteroides and was shown to contain three subunits. The first 42 amino acids of the β subunit were identified, as well as an internal peptide sequence spanning some 20 amino acids into the α subunit. Using degenerated primers from these sequences, we amplified a 1.2-kb DNA fragment by PCR from Leuconostoc mesenteroides subsp. cremoris . This fragment was used as a probe for screening a Leuconostoc genomic bank to identify the structural genes. The 2.7-kb gene cluster encoding citrate lyase of L. mesenteroides is organized in three open reading frames, citD , citE , and citF , encoding, respectively, the three ci…

DNA BacterialATP citrate lyaseMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeMicrobiologyBacterial ProteinsCarbon-Sulfur LigasesMultienzyme ComplexesGene clusterAcyl Carrier ProteinEscherichia colimedicineLeuconostocAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliBase SequenceSequence Homology Amino AcidStructural geneOxo-Acid-LyasesSequence Analysis DNALyasebiology.organism_classificationEnzymes and ProteinsMolecular biologyOxaloacetate decarboxylaseBiochemistryGenes BacterialLeuconostoc mesenteroidesMultigene FamilyCoenzyme A-TransferasesLeuconostoc
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