The Autolysis of Clostridium sporogenes

Galli, E.; Hughes, D. E.

doi:10.1099/00221287-39-3-345

Cited by 5 publications

(4 citation statements)

References 16 publications

(9 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The cell-wall membranes from a wide range of aerobically grown bacteria have also been found to have an ATPase similar to that reported here, and the enzyme has also been found in membrane preparations from Streptococcus faecalis ( Abrams, McNamara & Johnson, 1960) and in preparations from L. casei supplied to us by Dr J. Shockman. More recently the enzyme has been found in cell-wall membranes and empty spheroplasts (' ghosts ') of Clostridium qporogenes (Galli & Hughes, 1965) and in particulate fractions of Chlorobium thio~u l~h a t o p h~~~m (Cole & Hughes, 1965). The hull preparations from L. urubivzosus contained from 7 to 11 yo total lipid of which the bulk appeared to be phospholipid since it contained about 4 yo phosphorus.…”

Section: Discussionmentioning

confidence: 99%

The Enzymic Activity of the Outer Shell of Lactobacillus arabinosus

Cole

Hughes

1965

Journal of General Microbiology

Self Cite

View full text Add to dashboard Cite

SUMMARYPreparations of the outer shell of Lactobacillus arabinosus were made by crushing the bacteria in a Hughes press and removing the cytoplasm by washing and centrifugation. Such preparations had none of the enzymes associated with flavin-mediated oxidation; they had consistently adenosine triphosphatase (ATPase) activity. The kinetics and other properties of this enzyme were studied. The evidence suggested that the enzyme was bound to the cytoplasmic membrane, the bulk of which appeared to be within the cell wall. The preparation was thus similar to that from obligate facultative aerobes and which, in contrast to the preparations from lactobacilli, contained enzymes associated with oxygen utilization mediated by the cytochrome hydrogen transport system. The bound ATPase had an optimum at pH 6.0 and was not markedly inhibited by ouabain or oligomycin: it was stimulated by 2,&dinitrophenol. It was thus different from ATPase associated with ion transport but similar to that from mitochondria1 membranes. There was no nucleotide pyrophosphorylase activity in the preparation but other nucleotide triphosphates and diphosphates and some inorganic phosphates were hydrolysed but at slower rates than was ATP.

show abstract

Section: Discussionmentioning

confidence: 99%

The Enzymic Activity of the Outer Shell of Lactobacillus arabinosus

Cole

Hughes

1965

Journal of General Microbiology

Self Cite

View full text Add to dashboard Cite

show abstract

“…The number of the phage-like particles, however,was very low in spite of the abrupt lysis induced by MC. The rapid lysis may be partly or mainly due to autolytic systems inherent in spore-bearing organisms (Altenbern and Stull, 1965; Galli and Hughes, 1965; Kawata and Takumi, 1971) rather than due to the direct effects of phage multiplication.…”

Section: Other Tests To Dixerentiate Types B and Dmentioning

confidence: 99%

Susceptibility to Mitomycin C and Lecithinase Activities of Clostridium Oedematiens (C. Novyi) Types B and D

Nakamura

Takematsu

Nishida

1975

Journal of Medical Microbiology

View full text Add to dashboard Cite

PLATE XVIIT is still technically difficult to distinguish some strains of Clostridium oedematiens (C. novyi) of types B and D (Rutter and Collee, 1969). Type-A strains of C. oedematiens produce a haemolytic lecithinase (the $oxin) which is distinct from the haemolytic lecithinase (@-toxin) produced by type-B and type-D strains. As type-D strains are known to produce more of the /?-toxin lecithinase than type-B strains, it was hoped to determine ranges of this lecithinase activity, here referred to as p-lecithinase, that would discriminate between the two types. In the course of studies on the lysogeny of clostridia (Kiritani et al., 1973; Shimamura et al., 1974), we found that type-D strains differed from type-B strains of C. oedematiens in their susceptibility t Q mitomycin C (MC). This was investigated further in the present study with a view to differentiating type-B and type-D strains. Since treatment of bacteria in the lysogenic state by MC induces multiplication of phage, and since lysogeny is sometimes related to bacterial toxigenicity, we also examined strains of C. oedematiens of types B and D in parallel for susceptibility to MC and for production of the /?-lecithinase. MATERIALS AND METHODSBacterial strains C. oedematiens type A . Toxigenic strains 77101, 77103, 37101, 37106, and 37110 and non-toxigenic strains 3-1 103,3-1105,3-1111, and 3-1 112 are stock strains isolated from soil by one of the authors in 1963 and typed by Nishida and Nakagawara (1964).

show abstract

“…Several bacterial species are known to possess autolytic enzymes (autolysins) which are capable of hydrolyzing cell wall components (10,16,18). In contrast to the well-characterized systems of Streptococcus and Bacillus species, relatively little is known about the autolysis of Clostridium species (9,12,26). In two recent papers (2, 25) we described the production and purification of an autolytic glycoprotein (molecular weight, 28,000) by Clostridium acetobutylicum in an industrial fermentation medium.…”

mentioning

confidence: 99%

Autolytic Activity and an Autolysis-Deficient Mutant of Clostridium acetobutylicum

Allcock

Reid

Jones

et al. 1981

Appl Environ Microbiol

View full text Add to dashboard Cite

The optimum conditions for autolysis and autoplast formation in Clostridium acetobutylicum P262 have been defined. Autolysis was optimal at pH 6.3 in 0.04 M sodium phosphate buffer, and the bacterium produced latent and active forms of an autolytic enzyme. The ability of cells to autolyze decreased sharply when cultures entered the stationary phase. Autoplasts were induced by 0.25 to 0.5 M sucrose and were stable in media containing sucrose, CaCl2, and MgCl2. A pleiotropic autolysis-deficient mutant (lyt-1) was isolated. The mutant produced less autolysin than did the parent P262 strain, and it had an altered cell wall which was more resistant to both its own and P262 autolysins. The mutant formed long chains of cells, and lysozyme was required for the production of autoplasts. Growth of the P262 strain or the lyt-1 mutant was inhibited by the same concentrations of penicillin, ampicillin, and vancomycin. The lyt-1 mutant strain treated with the minimum growth-inhibitory concentration of penicillin autolyzed upon the addition of wild-type autolysin to the autolysis buffer at the same rate as did the untreated P262 strain. Chloramphenicol did not protect the penicillin-treated lyt-1 cells against autolysis enhanced by exogenous wild-type autolysin.

show abstract

The Autolysis of Clostridium sporogenes

Cited by 5 publications

References 16 publications

The Enzymic Activity of the Outer Shell of Lactobacillus arabinosus

The Enzymic Activity of the Outer Shell of Lactobacillus arabinosus

Susceptibility to Mitomycin C and Lecithinase Activities of Clostridium Oedematiens (C. Novyi) Types B and D

Autolytic Activity and an Autolysis-Deficient Mutant of Clostridium acetobutylicum

Contact Info

Product

Resources

About