Dependence of the viability and mutability of Escherichia coli K-12 cells on the balance of DNA and protein syntheses. II. The effect of disturbance in the balance of DNA and protein syntheses on the cellular mutability and viability of rec+ and rec- strains treated with nalidixic acid]

The changes in the survival and mutagenesis of rec+ and rec- Escherichia coli K-12 strains, treated with the selective inhibitor of DNA synthesis, nalidixic acid, are found to be due to the processes of the stabilization and repair of the metabolic gaps in DNA chains, which depend on the balance of DNA and protein synthesis. The various character is observed of the relation between the survival and the mutagenesis and the balance of DNA and protein syntheses in cells which are valuable (rec+) and defective (rec-) for the processes of DNA repair.     

The sequence of beta A - and beta B-chains from carp hemoglobins (Cyprinus carpio L.)]

The primary structures of the beta A - and beta B-chains from the both main components of carp hemoglobins is given. The sequence was established by splitting with known methods and sequencing the products using the hydrophilic and hydrophobic programmes in the sequenator. The carp beta-chains differ from human beta-chains in the exchange of 66 and 67 amino acid residues, respectively; the beta A - beta B-chains differ by 4 amino acids (pos. no. 13, 41, 122 and 143). Both chains have one insertion in the position 121 or 122. The results are discussed.     

Kinetic investigation of the interaction of cibacron blue F3G-A with phosphofructokinase from yeast.

Yeast phosphofructokinase is strongly inhibited by Cibacron Blue F3G-A. The inhibition is competitive in respect to the phosphate donor. Fructose 6-phosphate and ATP are able to abolish the dye-inhibition. Replacement of the strong inhibitor ATP by ITP as phosphate donor gives qualitatively analogous effects. The influence of Cibacron Blue F3G-A on the kinetic pattern of yeast phosphofructokinase can be described in terms of the kinetic model of Freyer et al. [8] if one assumes that the dye binds to the ATP-binding sites in a competitive manner.     

Submitochondrial localization and function of alkaline inorganic pyrophosphatase in maize seedlings.

Alkaline inorganic pyrophosphatase and Mg-ATPase are localized within the mitoplast of maize seeding mitochondria. NaF inhibited the PPase activity, whereas oligomycin and dicyclohexylcarbodiimide inhibited the Mg-ATPase activity. The mitoplast preparation synthesized PPi from Pi under conditions excluding hydrolysis of endogenous ATP. PPi synthesis was inhibited by ADP, antimycin A, NaCN and 2,4- dinitrophenol but not by oligomycin. It is suggested that PPi synthesis in the maize seedling mitochondria proceeds at the expense of the energy of electron transport chain and is independent of the ATP synthesis.     

Re-examination of the subcellular localization of thyroxine 5''-deiodination in rat liver.

We describe the existence of at least two thyroxine 5'-deiodinases in rat liver. They co-fractionate with NADPH-cytochrome c reductase, the marker enzyme for membranes of the endoplasmic reticulum. Subcellular-localization studies of the most active microsomal thyroxine 5'-deiodinase were performed under substrate saturation and at optimal pH 6.8. This enzyme was a Km(app.) of about 3 microM-thyroxine and a Vmax. of about 8 ng of tri-iodothyronine/min per mg of protein. Our study confirms in part the earlier reports of microsomal localization of thyroxine 5'-deiodination. However, this process is not mediated by only a single enzyme.     

Uptake of immune RNA by normal mouse spleen cells

Summary Normal mouse spleen cells take up in vitro radioactively labeled immune RNA. RNA taken up is present in nuclei, polysomes, membranes and cytoplasm. About 20–40% of immune RNA is nonspecifically associated with cell surface. 45% of RNA taken up is degraded and reutilized inside the cells within 2 hours.This work was supported by the Polish Academy of Sciences within the project 09.7.4.1.1.     

The nucleotide sequence of tRNA tyrosine from the fission yeast Schizosaccharomyces pombe.

The sequence of tRNA tyrosine from the fission yeast Schizosaccharomyces pombe is pCUCCUGAUm1 GGUG psi AGDDGGDDAUCACACor (psi) CCGGUG psi Ai6 AACCGGUUGm7 GUm5C GCUAGT psi CGm1 AUUCUGGUCAGGAGACCAOH. This sequence differs in 30 nucleotides from the tRNA-Tyr seqence of the budding yeast Saccharomyces cerevisiae. It has a unique anticodon stem of only four GC base pairs. The normal fifth pair position of nucleotide 28-44 is occupied by a C-U and in 20% of the tRNA-Tyr molecules it is psi-U. This unusual feature and its implications are considered in the discussion.