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PubMed1981

[DNA-methylase from Arthrobacter luteus screens DNA from the action of site-specific endonuclease Alu I].

DNA-methylase was isolated from a cell extract of A. luteus and partially purified by chromatography on phosphocellulose. The purified enzyme methylates DNA of phage lambda and plasmids pBr322, thus making them resistant to a subsequent action of endonuclease Alu I. It has been shown that cytosine is the object of methylation within DNA. This modification does not screen DNA from the action of site-specific endonucleases Sal I, Bam HI, EcoR I, EcoR II, Xho I and Xho II. It has been experimentally demonstrated that the isolated methylase is site-specific and identifies in the DNA the nucleotide sequence 5'-AGCT-3', by methylating cytosine in the DNA.

Arthrobacter↗
PubMed1983

[Coupling between 3-ketosteroid-delta'-dehydrogenase and the respiratory chain in the bacterium Arthrobacter globiformis].

Intact bacterial cells and their cytoplasmic membranes obtained by ultrasonic desintegration are able to induce dehydration of hydrocortisone to prednisolone that is coupled with O2 uptake. This reaction is inhibited by cyanide and 2-n-nonyl-4-hydroxyquinoline-N-oxide (HOQNO). Oxidation of hydrocortisone results in cytochrome reduction both in intact cells and in cytoplasmic membranes. Aerobic dehydration of hydrocortisone is linked with transmembrane potential generation. The data obtained suggest that the electron translocation from 3-ketosteroid-delta'-dehydrogenase to O2 occurs via the respiratory chain. The enzyme donates reduced equivalents directly to the respiratory chain, presumably at the level of menaquinone.

Arthrobacter↗