Etude du rôle du kinétoplaste dans le métabolisme de crithidia luciliae

Doctorat en Sciencesinfo:eu-repo/semantics/nonPublishe

Existence of two distinct protein synthesis systems in the trypanosomatid Crithidia luciliae

Crithidia luciliae has a single mitochondrion which occupies a large part of the cell. Two different types of ribosomes have been isolated from the cell: cytoplasmic 83 S and mitochondrial 60 S. The 83-S ribosomes are dissociated by Mg2+ at 10-3 mM into their subunits 62 S and 46 S. The 60-S ribosomes, obtained from the mitochondria, are easily dissociated into 45-S and 32-S subunits at higher concentrations of Mg2+ (3 mM). By these methods, an unusually large amount of mitochondrial ribosomes in Crithidias are found. The biosynthetic activity of the cytoplasmic and the mitochondrial ribosomes and their sensitivity to specific protein synthesis inhibitors (chloramphenicol, erythromycin, cycloheximide) has been studied in vitro. © 1974.SCOPUS: ar.jinfo:eu-repo/semantics/publishe

Étude des effets de l'acriflavine et du bromure d'éthidium sur l'incorporation de précurseurs radioactifs dans les acides nucléiques et les protéines du trypanosomide "crithidia luciliae"

info:eu-repo/semantics/publishe

Accounting for protein subcellular localization:A compartmental map of the rat liver proteome

Accurate knowledge of the intracellular location of proteins is important for numerous areas of biomedical research including assessing fidelity of putative protein-protein interactions, modeling cellular processes at a system-wide level and investigating metabolic and disease pathways. Many proteins have not been localized, or have been incompletely localized, partly because most studies do not account for entire subcellular distribution. Thus, proteins are frequently assigned to one organelle whereas a significant fraction may reside elsewhere. As a step toward a comprehensive cellular map, we used subcellular fractionation with classic balance sheet analysis and isobaric labeling/quantitative mass spectrometry to assign locations to >6000 rat liver proteins. We provide quantitative data and error estimates describing the distribution of each protein among the eight major cellular compartments: nucleus, mitochondria, lysosomes, peroxisomes, endoplasmic reticulum, Golgi, plasma membrane and cytosol. Accounting for total intracellular distribution improves quality of organelle assignments and assigns proteins with multiple locations. Protein assignments and supporting data are available online through the Prolocate website (http://prolocate.cabm.rutgers.edu). As an example of the utility of this data set, we have used organelle assignments to help analyze whole exome sequencing data from an infant dying at 6 months of age from a suspected neurodegenerative lysosomal storage disorder of unknown etiology. Sequencing data was prioritized using lists of lysosomal proteins comprising well-established residents of this organelle as well as novel candidates identified in this study. The latter included copper transporter 1, encoded by SLC31A1, which we localized to both the plasma membrane and lysosome. The patient harbors two predicted loss of function mutations in SLC31A1, suggesting that this may represent a heretofore undescribed recessive lysosomal storage disease gene

Différences socio-culturelles et éducation optimisée en milieu scolaire de deux à 7-8 ans

Als conclusie kan gesteld worden dat het van belang is, enerzijds, om op alle niveaus van het schoolsysteem een gedifferentieerde en optimale aanpak te ontwikkelen, en anderzijds om onderwijs en sociale problemen in samenhang te behandelen. Democratisering van het onderwijs kan zich niet afzonderlijk van de maatschappij ontwikkelen