Search results for "Protein-fragment complementation assay"

showing 5 items of 5 documents

CitA (citrate) and DcuS (C4-dicarboxylate) sensor kinases in thermophilic Geobacillus kaustophilus and Geobacillus thermodenitrificans

2015

The thermophilic Geobacillus thermodenitrificans and Geobacillus kaustophilus are able to use citrate or C4-dicarboxylates like fumarate or succinate as the substrates for growth. The genomes of the sequenced Geobacillus strains (nine strains) each encoded a two-component system of the CitA family. The sensor kinase of G. thermodenitrificans (termed CitAGt) was able to replace CitA of Escherichia coli (CitAEc) in a heterologous complementation assay restoring expression of the CitAEc-dependent citC-lacZ reporter gene and anaerobic growth on citrate. Complementation was specific for citrate. The sensor kinase of G. kaustophilus (termed DcuSGk) was able to replace DcuSEc of E. coli. It respon…

0301 basic medicineMolecular Sequence Data030106 microbiologyHeterologousBacillus subtilismedicine.disease_causeMicrobiologyGeobacillusCitric Acid03 medical and health sciencesBacterial ProteinsProtein-fragment complementation assaymedicineDicarboxylic AcidsAmino Acid SequenceEscherichia colibiologyThermophileGeobacillusGene Expression Regulation Bacterialbiology.organism_classificationComplementationBiochemistryHeterologous expressionProtein KinasesSequence AlignmentMicrobiology
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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

2016

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the inserti…

0301 basic medicineProtein familyCèl·lulesBiologyBiochemistryMitochondrial Proteins03 medical and health sciencesProtein DomainsMembranes (Biologia)Protein-fragment complementation assayMembrane BiologyMicrosomesProto-Oncogene ProteinsHumansMolecular BiologyAdaptor Proteins Signal TransducingGeneticsBcl-2-Like Protein 11030102 biochemistry & molecular biologyCell MembraneBcl-2 familyProteïnes de membranaMembrane ProteinsBiological membraneCell BiologyFusion proteinTransmembrane proteinCell biology030104 developmental biologyMembraneProto-Oncogene Proteins c-bcl-2Membrane proteinB-cell lymphoma 2 (Bcl-2) family BH3-only apoptosis membrane insertion membrane protein mitochondrial apoptosis transmembrane domainApoptosis Regulatory ProteinsHydrophobic and Hydrophilic InteractionsHeLa CellsJournal of Biological Chemistry
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Differences in the Association of BH3-Only Proteins to Biological Membranes

2017

Apoptosis, a prevalent mechanism of programmed cell death, is regulated by the Bcl-2 protein family. The balance between pro- and anti-apoptotic Bcl-2 members in the mitochondrial outer membrane (MOM) protects or triggers MOM permeabilization. Bcl-2 homology-3 (BH3)-only proteins participate in this process activating pro-apoptotic effectors and promoting permeabilization of the MOM. The membrane association of BH3-only proteins is controversial due to the lack of a canonical carboxyl-terminal (C-terminal) transmembrane (TM) domain. We used an in vitro transcription/translation system to study the insertion capacity of these hydrophobic C-terminal regions of the BH3-members Bik, Bim, Noxa, …

MembraneProtein familyProtein-fragment complementation assayBcl-2 familyBiophysicsBiological membraneBiologyBacterial outer membraneTransmembrane proteinCell biologyGreen fluorescent proteinBiophysical Journal
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Extraction and Analysis of Carotenoids from Escherichia coli in Color Complementation Assays

2017

A common method to investigate the function of genes putatively involved in carotenoid biosynthesis is the so called color complementation assay in Escherichia coli (see, e.g., Cunningham and Gantt, 2007). In this assay, the gene under investigation is expressed in E. coli strains genetically engineered to synthesize potential carotenoid substrates, followed by analysis of the pigment changes in the carotenogenic bacteria via high-performance liquid chromatography (HPLC). Two crucial steps in this method are (i) the quantitative extraction of the carotenoids out of E. coli and (ii) the reproducible and complete separation of the pigments by HPLC. Here, we present a protocol for the extracti…

0106 biological sciences0301 basic medicineLuteinStrategy and Managementmedicine.disease_cause01 natural sciencesIndustrial and Manufacturing Engineering03 medical and health scienceschemistry.chemical_compoundProtein-fragment complementation assayMethods ArticlemedicineCarotenoidEscherichia colichemistry.chemical_classificationChromatographyMechanical EngineeringExtraction (chemistry)Metals and Alloysfood and beveragesComplementationZeaxanthin030104 developmental biologychemistryXanthophyll010606 plant biology & botanyBIO-PROTOCOL
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Characterization of the Copper Transporters from Lotus spp. and Their Involvement under Flooding Conditions

2019

Forage legumes are an important livestock nutritional resource, which includes essential metals, such as copper. Particularly, the high prevalence of hypocuprosis causes important economic losses to Argentinian cattle agrosystems. Copper deficiency in cattle is partially due to its low content in forage produced by natural grassland, and is exacerbated by flooding conditions. Previous results indicated that incorporation of Lotus spp. into natural grassland increases forage nutritional quality, including higher copper levels. However, the biological processes and molecular mechanisms involved in copper uptake by Lotus spp. remain poorly understood. Here, we identify four genes that encode p…

0106 biological sciences0301 basic medicineBiologíalegumesLotusCOPPERFLOODING01 natural scienceslcsh:ChemistryCopper transportersProtein-fragment complementation assayCation Transport Proteinslcsh:QH301-705.5SpectroscopyPlant Proteinsbiologyfood and beveragesGeneral MedicinePhenotypeComputer Science ApplicationsLEGUMESSaccharomyces cerevisiaechemistry.chemical_elementCatalysisArticleInorganic Chemistry03 medical and health sciencesfloodingStress PhysiologicalFORAGEBotanymedicineCiencias AgrariasPhysical and Theoretical ChemistryMolecular BiologyGeneOrganic Chemistryfungiforagebiology.organism_classificationmedicine.disease//purl.org/becyt/ford/4.5 [https]CopperTRANSPORTERScopper transportersYeastFloods030104 developmental biologychemistrylcsh:Biology (General)lcsh:QD1-999CIENCIAS AGRÍCOLASLotusOtras Ciencias AgrícolasCopper deficiency//purl.org/becyt/ford/4 [https]Copper010606 plant biology & botanyInternational Journal of Molecular Sciences
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