Cell protein profiles of submerged cultures of Streptomyces aureofaciens cultivated in the absence or presence of 12 microM benzyl thiocyanate (BT) were analyzed by one-dimensional SDS polyacrylamide gel electrophoresis. Substantial increase in the intensity of the 13, 35, 37, 60, and 100 kDa protein bands was observed in cultures treated with BT. Similar increase in the 35, 37, and 60 kDa bands was found in a mutant blocked in the last chlortetracycline biosynthesis step. Effect of BT on the solid medium-grown cultures was also observed, with a more intensive substrate mycelium pigmentation and alteration in the spore size and shape as the most characteristic features. Earlier studies of BT effect involving those on the stimulation of chlortetracycline biosynthesis are summarized and a possible signal-transducing mechanism is discussed from the point of view of adaptation of S. aureofaciens to the uncoupling of oxidative phosphorylation.

• MeSH
• Bacterial Proteins metabolism   MeSH
• Microscopy, Electron MeSH
• Streptomyces aureofaciens drug effects   metabolism   ultrastructure   MeSH
• Tetracyclines biosynthesis   MeSH
• Thiocyanates pharmacology   MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Bacterial Proteins MeSH
• benzyl thiocyanate MeSH Browser
• Tetracyclines MeSH
• Thiocyanates MeSH

Mycelia of a low- and a high-production strain of Streptomyces aureofaciens were converted into protoplasts and divided into five subcellular fractions in order to localize exopolyphosphatases (EC 3.6.1.11), triphosphatase (EC 3.6.1.25), inorganic diphosphatase (EC 3.6.1.1), apyrase (EC 3.6.1.5) and glucokinase (EC 2.7.1.2). The highest specific activity of enzymes hydrolyzing polyphosphates was found in cytoplasmic vesicles and membranes. Triphosphatase was detected in the periplasmic fraction. Periplasmic vesicles and cytoplasm exhibited a high activity of diphosphatase. Apyrase was found mainly in the fractions of membranes and cytoplasmic vesicles. Glucokinase was a cytoplasmic enzyme. The enzymes were released from membrane structures into cytoplasm or periplasmic space if benzyl thiocyanate (10 microM) was present in the growth medium.

• MeSH
• Potassium pharmacology   MeSH
• Phosphoric Monoester Hydrolases metabolism   MeSH
• Glucokinase metabolism   MeSH
• Magnesium pharmacology   MeSH
• Cations MeSH
• Kinetics MeSH
• Sodium pharmacology   MeSH
• Streptomyces aureofaciens drug effects   enzymology   MeSH
• Subcellular Fractions enzymology   MeSH
• Thiocyanates pharmacology   MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• benzyl thiocyanate MeSH Browser
• Potassium MeSH
• Phosphoric Monoester Hydrolases MeSH
• Glucokinase MeSH
• Magnesium MeSH
• Cations MeSH
• Sodium MeSH
• Thiocyanates MeSH