H. W. Schaup

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The effect of 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) on acetyl-CoA carboxylase (ACC) activity and synthesis was examined. Male Wistar rats received a singlei. p. injection of TCDD (53 μg/kg), and nine days later body weight, liver weight, hepatic lipid, ACC activity and mass were determined and compared to pair-fed controls. Body weights of TCDD-treated(More)
The catalog of oligomers produced by ribonuclease T1 digestion ofEscherichi coli 16S ribosomal RNA has been determined by a new method that involves the use of ribonuclease U2 fromUstilago sphaerogena. The sequences for the larger T1 oligomers (8 or more bases) determined in this way differ in more than 50 % of the cases from those reported previously(More)
Protein synthesis, which takes place within ribosomes, is essential for the survival of any living organism. Ribosomes are composed of both proteins and RNA. Specific interaction between the 3' end CCUCC sequence of prokaryotic 16S rRNA and a partially complementary sequence preceding the initiating codon of mRNA is believed to be a prerequisite for(More)
A portion of the 16S ribosomal RNA that binds specifically to, and is protected from nucleolytic attack by, ribosomal protein S4 has been characterized in terms of its partial primary structure. The specific RNA (S4aR) in question comprises slightly more than onefourth of the full 16S molecule, and appears to be located (at least in part) in the 5′-proximal(More)
Five of the 30S ribosomal proteins from E. coli were tested for their ability to bind to 16S ribosomal RNA. Only one of these, S15, can form a complex with the RNA. Quantitative measurements as well as competition experiments show that the RNA binding site for the attachment of S15 is specific for this protein. These experiments complete our analysis of all(More)
The interaction between ribosomal proteins of the 30s subunit with intact 50s subunits was investigated. Experiments with mixtures of total 30s proteins indicated that several 30s proteins including protein s4 would form a stable complex with 50s subunits. Further work with pure s4 indicates that this protein binds stoichiometrically to the 50s subunits,(More)
Ribosomes play an active role in protein biosynthesis. Ribosomal RNA conformation in ribosomal subunits, intramolecular interactions between different rRNA sequences within the confinement of the particles, and intermolecular interactions are presumed necessary to support efficient and accurate protein synthesis. Here we report an analysis of the(More)