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PubMed1965

PLASMOLYSIS IN BACILLUS MEGATERIUM.

Weibull, Claes (Central Bacteriological Laboratory of Stockholm City, Stockholm, Sweden). Plasmolysis in Bacillus megaterium. J. Bacteriol. 89:1151-1154. 1965.-Sucrose solutions stronger than 1 m caused plasmolysis in Bacillus megaterium strain M, whereas concentrated NaCl and KNO(3) solutions were ineffective. In plasmolyzed cells, mesosome bodies were found in pockets between the cytoplasmic membrane and the cell wall. After plasmolysis, the cytoplasmic membrane appeared as a triple-layered structure, a "unit membrane." Plasmolysis did not markedly influence the viability of the cells.

Bacillus megaterium↗
PubMed1965

LYSIS OF BACTERIAL PROTOPLASTS AND SPHEROPLASTS BY STAPHYLOCOCCAL ALPHA-TOXIN AND STREPTOLYSIN S.

Bernheimer, Alan W. (New York University School of Medicine, New York, N.Y.), and Lois L. Schwartz. Lysis of bacterial protoplasts and spheroplasts by staphylococcal alpha-toxin and streptolysin S. J. Bacteriol. 89:1387-1392. 1965.-Protoplasts of Bacillus megaterium, Sarcina lutea, and Streptococcus pyogenes, and spheroplasts of Escherichia coli were lysed by staphylococcal alpha-toxin, whereas spheroplasts of Vibrio metschnikovii and V. comma were not. In the spectrum of its lytic action, streptolysin S qualitatively resembled staphylococcal alpha-toxin except for failure to lyse S. pyogenes protoplasts. In contrast to the two foregoing agents, streptolysin O did not lyse protoplasts and spheroplasts. The observations are interpreted in relation to similarities and differences in lipid composition of bacterial and mammalian cell membranes.

Animals↗
PubMed1965

NATURE OF THE BACTERICIDAL ACTION OF ANTIMYCIN A FOR BACILLUS MEGATERIUM.

Marquis, Robert E. (University of Rochester, Rochester, N.Y.). Nature of the bactericidal action of antimycin A for Bacillus megaterium. J. Bacteriol. 89:1453-1459. 1965.-Antimycin A, a fungicidal antibiotic which specifically inhibits metabolic reduction of cytochrome c, was found to be lethal for Bacillus megaterium. However, the bactericidal action was correlated with a capacity of antimycin to hinder plasma-membrane functions other than cytochrome-mediated respiration. With conditions under which oxygen consumption was not appreciably depressed, antimycin almost completely inhibited concentrative uptake of both alpha-aminoisobutyrate and alpha-methylglucoside, and also caused death of cells. When present in amounts greater than those required for killing or for inhibition of nutrilite uptake, antimycin also induced extensive loss of inorganic phosphate and other substances from whole cells, inhibited aerobic respiration, and acted as a lytic agent for isolated protoplasts. The lytic potency of antimycin was greater, on a molar basis, than that of digitonin, hexachlorophene, polymyxin B, and all but one of a number of test detergents. Protoplasts concentrated antimycin primarily in or on the plasma membrane, and the refractive index of isolated protoplast membranes rose sharply as a result of antimycin binding. In all, antimycin-induced lysis appeared not to include dissolution of the protoplast membrane similar to that produced by dodecyl sulfate. Rather, the lytic process seemed more akin to that induced by cationic detergents or by polymyxin.

Aminoisobutyric Acids↗
PubMed1965

LYSIS OF BACTERIAL CELL WALLS BY AN ENZYME ISOLATED FROM A MYXOBACTER.

Ensign, J. C. (University of Illinois, Urbana), and R. S. Wolfe. Lysis of bacterial cell walls by an enzyme isolated from a myxobacter. J. Bacteriol. 90:395-402. 1965.-An exoenzyme which lyses intact cells, heat-killed cells, and cell walls of Arthrobacter crystallopoietes was purified 60-fold from the growth liquor obtained from a myxobacter (strain AL-1). The lytic enzyme was produced during growth of the organism in a number of complex media, the maximal amount of enzyme being produced in yeast extract broth. The purified enzyme lysed at different rates a number of gram-positive bacteria. With the exception of Rhodospirillum rubrum, Spirillum itersonii, and S. serpens, the gram-negative bacteria tested were not attacked.

Arthrobacter↗
PubMed1965

EVIDENCE OF LYSOGENY IN DERIVATIVES OF ESCHERICHIA COLI.

Frampton, E. W. (The University of Texas M. D. Anderson Hospital and Tumor Institute, Houston), and B. R. Brinkley. Evidence of lysogeny in derivatives of Escherichia coli. J. Bacteriol. 90:446-452. 1965.-Exposure of cultures of several thymine-requiring derivatives of Escherichia coli strain 15 to radiation [X rays or ultraviolet (UV)] resulted in an increased synthesis of ribonucleic acid (RNA) as measured by the incorporation of radioactive uridine. In addition to radiation, mitomycin C (5 or 25 mug/ml) or growth in the absence of thymine also stimulated RNA synthesis in cultures in which the bulk of RNA synthesis was terminated by a shift-down in growth conditions. RNA purified from X-irradiated bacteria was resolved on columns of methylated serum albumin and yielded an elution profile which appeared similar to RNA synthesized by phage-infected bacteria. Electron microscopic examination of cultures induced to lyse by exposure to UV radiation, or by growth in the presence of 5-bromouracil before exposure to radiation (X rays or UV), showed the presence of mostly incomplete phage particles.

Bacteriolysis↗
PubMed1965

BINDING OF RIBOSOMES TO CYTOPLASMIC RETICULUM OF BACILLUS MEGATERIUM.

Schlessinger, David (Washington University School of Medicine, St. Louis, Mo.), Vincent T. Marchesi, and Benjamin C. K. Kwan. Binding of ribosomes to cytoplasmic reticulum of Bacillus megaterium. J. Bacteriol. 90:456-466. 1965.-As many as 60% of the cellular ribosomes are bound to membrane "ghosts" in lysozyme lysates in 0.02 m Mg(2+). Bound ribosomes labeled with C(14)-uracil do not exchange with added unlabeled ribosomes, even after disruption of the cell membrane by sonic treatment. Electron micrographs of thin sections of ghosts, or of fragments produced by sonic disruption of protoplasts, indicate that the ribosomes are distributed on a reticular matrix which extends throughout the cytoplasm. The binding of ribosomes to this matrix is insensitive to ribonuclease or deoxyribonuclease, and has many other features in common with the binding of ribonucleoprotein to the membranous elements of the mammalian microsomal fraction, though the reticulum does not appear to be membranous. Thus, functioning ribosomes may be bound to a cytoplasmic structure in all cell types.

Bacillus megaterium↗