14 research outputs found
A 15-kD Interferon-Induced Protein and Its 17-kD Precursor: Expression in Escherichia coli
Differences in electrophoretic behaviour of eight ribosomal proteins from rat and rabbit tissues and evidence for proteolytic action on liver proteins
Retinoic acid-inducible gene-I is induced by interferon-γ and regulates the expression of interferon-γ stimulated gene 15 in MCF-7 cells
Characterization of Cystatin C from Bovine Parotid Glands: Cysteine Proteinase Inhibition and Antiviral Properties
Expression of Cathepsin P mRNA, Protein and Activity in the Rat Choriocarcinoma Cell Line, Rcho-1, During Giant Cell Transformation
Mengo virus 3C proteinase: Recombinant expression, intergenus substrate cleavage and localizationin vivo
Organization and expression of a two-gene cluster in the arginine biosynthesis of Saccharomyces cerevisiae
In Saccharomyces cerevisiae, argB and argC define two adjacent and complementing loci, with mutants defective in two consecutive steps of arginine biosynthesis: N-acetylglutamate kinase (AG-kinase) and N-acetylglutamyl-phosphate reductase (AGPreductase). These enzymic activities are readily separated by ammonium sulfate fractionation or Sephadex G-200 chromatography. This suggests that each activity is carried in vivo by a different protein. The synthesis of the two enzymes is coordinately regulated, with an 85-fold difference in specific activities between fully repressed and fully derepressed cells. Missense mutations in the argB locus are defective in AGkinase only. Nonsense mutations in the argB locus are defective in both activities. Missense and nonsense mutations in the argC locus are defective in AGPreductase, with a few alleles also showing a reduced level of AGkinase. These data are best explained by assuming that argB and argC are two genes transcribed as a single messenger from argB to argC. This messenger produces in vivo two distinct proteins corresponding to the argB and argC gene products, either because translation can be initiated at the beginning of both genes, or because a large polypeptide is specifically cut in vivo to yield the gene products of argB and argC. © 1979 Springer-Verlag.SCOPUS: ar.jinfo:eu-repo/semantics/publishe