DNA methylation in wheat. Purification and properties of DNA methyltransferase.

The origin and function of the large amount of 5-methylcytosine in plant DNA is not well understood. As a tool for in vitro studies of methylcytosine formation in plants we have isolated and characterized the DNA methyltransferase present in germinating wheat embryo. An enzyme fraction enriched 300-fold over the tissue homogenate was obtained by salt extraction of nuclei, chromatography on DEAE-cellulose, Sephadex G-75, blue Sepharose and on DNA immobilized on cellulose.

Unexpected specificity in the thioredoxin activation of fructose-bis-phosphatases from different plants.

Green seedlings of soy bean and wheat contain, like the plant seeds, multiple thioredoxin proteins which possess all typical thioredoxin properties but are inactive in the stimulation assay with spinach fructose-bis-phosphatase. However the pure proteins do have thioredoxin f activity when tested with homologous enzymes isolated from soy bean or wheat leaves, respectively, in the presence of Mg++. This new type of species specificity, unknown in all other in vitro assays of reduced thioredoxins, has to be considered in characterizing complete thioredoxin profiles in plants.

Aurintricarboxylic acid and polynucleotides as novel inhibitors of ribonucleotide reductases.

Ribonucleoside diphosphate reductases isolated from Escherichia coli, baker's yeast, Ehrlich ascites tumor cells, and unicellular green alga (Scenedesmus obliquus) are inhibited strongly and uniformly by the polymeric triphenylmethane dye, aurintricarboxylic acid. The molecule appears to interact simultaneously with the enzyme's various nucleotide and catalytic (iron-organic radical) sites. Oligo- and polyribonucleotides are also inhibitory.