PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Megacins”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 19 recordsLinked to original sources
PubMed1989

A new bacteriocinogenic activity: megacin BII encoded by plasmid pSE 203 in strains of Bacillus megaterium.

Mesophilic strains producing a new bacteriocin: Megacin BII, have been isolated from strains of Bacillus megaterium. Facultatively thermophilic strains producing Megacin BI were less sensitive to this new activity than non-producing mesophiles and strains producing Megacin BII were also more resistant to Megacin BI. Strains producing Megacin BII contained a large plasmid of 36.10(6):pSE 203. This plasmid was introduced into non-megacinogenic acceptor strains by protoplast transformation, they then became megacin producers and immune to Megacin BII. Plasmid pSE 203 has been mapped with endonucleases. No similarity to the Megacin A plasmids pBM 309 [Rostás et al. (1980) and pBM 113 (von Tersch and Carlton (1983 b)] was evident.

Autoradiography↗
PubMed1983

Bacteriocin from Bacillus megaterium ATCC 19213: comparative studies with megacin A-216.

A bacteriocin produced by Bacillus megaterium ATCC 19213 was identified, purified, and compared with megacin A from B. megaterium 216. The ATCC 19213 bacteriocin was inducible with mitomycin C and showed phospholipase A activity. Both megacin A-216 and megacin A-19213 contained two dissimilar polypeptide subunits. Megacin A-216 contains a 30,000-dalton alpha subunit and a 15,000-dalton beta subunit. Megacin A-19213 is composed of an alpha subunit 18,000 daltons in mass and a beta subunit about 7,500 daltons in mass. No sequence similarities between alpha and beta subunits of either megacin were detected. The two megacins were further distinguished by quantitative differences in activity spectra and by immunodiffusion analyses.

Bacillus megaterium↗
PubMed1977

Production of megacins C and Cx: presumptive evidence extrachromosomal control.

Exposure of growing cultures of Bacillus megaterium C4A(-) to ethidium bromide or an elevated growth temperature was found to eliminate megacin C production. Ethidium bromide resulted in a cure rate of up to 13%. Growth at 43 degrees C gave a cure rate of up to 99%. Megacin C production was lost spontaneously at a rate of 4% or less. There was a greater rate of spontaneous loss of megacin Cx production by B. megaterium 337, up to 14%. Growth at 43 degrees C resulted in a cure rate of up to 24% in this organism. Reversion to the Meg(+) state by cured clones has never been demonstrated. These observations support the hypothesis that production of megacins C and Cx is plasmid mediated. Meg(-) clones adsorbed more megacin than either parent strain and were more susceptible to megacin action.

Bacillus megaterium↗
PubMed1981

Improved purification and some properties of megacin Cx, a bacteriocin produced by Bacillus megaterium.

Megacin Cx is a bacteriocidal protein, previously described by Durner and Mach (Durner, K. (1970) Z. Allg. Mikrobiol. 10, 93-102; Durner, K. (1970) Z. Allg. Mikrobiol. 10, 373-382; Durner, K., and Mach, F. (1966) Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. Abt. I Orig. 2, 120, 565-575), which is released into the medium during growth by Bacillus megaterium strain 337. We have optimized the culturing conditions to achieve reproducibly high yields of this protein; under these conditions, megacin Cx represents about one-half of the protein secreted into the medium. We have developed improved methods of purifying the protein to homogeneity. The active form of megacin Cx is a monomeric protein, a single polypeptide of Mr = 210,000, as determined by analytical ultracentrifugation and gel electrophoresis in sodium dodecyl sulfate. Like many other proteins secreted by Gram-positive organisms, megacin Cx contains remarkably little methionine and cysteine. The purified protein blocks protein synthesis in sensitive cells, but has little immediate effect upon nucleic acid synthesis. Our purification procedure separates megacin Cx from another activity in the culture medium which blocks the synthesis of RNA and DNA, as well as synthesis of protein, in sensitive cells.

Amino Acids↗
PubMed1984

Molecular cloning of structural and immunity genes for megacins A-216 and A-19213 in Bacillus megaterium.

A host-vector system was developed for molecular cloning in Bacillus megaterium and used to clone the structural and immunity genes for megacins A-216 and A-19213. Recombinant clones that expressed immunity only or both immunity to and production of each megacin were obtained. Restriction mapping of native megacinogenic plasmids and recombinant clones was used to construct physical and genetic maps of megacinogenic plasmids pBM309 and pBM113. Limited sequence homology between pBM309 and pBM113 was detected by Southern blot hybridization and was mapped to, at most, a 6.4-kilobase-pair region of pBM309 and a 6.1-kilobase-pair region of pBM113.

Bacillus megaterium↗
PubMed1975

Electron microscopy of phages liberated by megacin A producing lysogenic Bacillus megaterium strains.

Mitomycin C was added at fairly high concentration (5-10 mug/ml) to exponentially growing cultures of selected strains of Bacillus megaterium. Lysis of the bacteria followed, associated by liberation of phage and megacin A production. In contrast, a low concentration (0.5 mug/ml) of mitomycin induced only megacin A production. Electron microscopic examination of the lysates induced by 5-10 mug/ml of mitomycin in 19 strains of B. megaterium showed them all to contain phages; most of the strains proved polylysogenic. Their lysates contained distinct complete phages of different structures and dimensions. A few strains released defective phage particles. The significance of the electron microscopic findings is discussed in relation to megacinogeny.

Bacillus megaterium↗
PubMed1976

Studies on megacinogeny in Bacillus cereus. I. Multiplication of phage wx causing lysogenic conversion to megacin A (phospholipase A) production.

Phage wx capable of reconverting Bacillus cereus strain W derivatives, cured to lose megacin A (phospholipase A) production into megacin A-producing cultures, exhibits unusual kinetics of multiplication; its clear mutant, phage wxc, behaves similarly. The phages are not adsorbed by stationary phase indicator bacteria. As sonicated bacteria fail to inactivate the phages, the absence of adsorption cannot be attributed to an undersurface localization of the receptors. Multiplying bacteria exert a slow and slight degree of phage adsorption. Cells inhibited by chloramphenicol produce no receptors. It has been assumed that the receptor, produced from a precursor involved in bacterial cell synthesis, either absorbs the phage in the nascent state or is incorporated in the cell and loses its phage-adsorbing capacity.

Adsorption↗
PubMed1976

Studies on megacinogeny in Bacillus cereus. II. Bacillus cereus isolates characterized by prophage-controlled production of megacin A (phospholipase A).

Five out of a number of Bacillus cereus strains isolated from soil produced high titre specific bacteriocin (megacin A) in mitomycin C-induced cultures. In the course of cultivation with ethidium bromide, the strains gave off segregants not producing bacteriocin (cin-). The lysate of two wild strains formed plaques on the corresponding cin- bacteria. The two phages (wx23 and wx26) were identical in antigenic structure with phage wx was present in the lysate of B. cereus strain W, and converted cin- derivatives into cultures producing megacin A (phospholipase A). The phages produced plaques at 26 degrees C but not at 37 degrees C. In the lysates of the remaining three strains phages were not detected with biological and morphological methods; these cultures have been assumed to carry defective prophage genome. As the corresponding prophages are responsible for the determination of inducible phospholipase A production, phages named wx seem to form a separate group of B. cereus phages.

Bacillus cereus↗
PubMed1959

Megacins.

Explore the source record for details and available documents.

Anti-Bacterial Agents↗