Vibrio mutants of Rhodospirillum rubrum.
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Alanine↗
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Results for “BACTERIOLYSIS”
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Role of cell wall antolysin in chain formation by a mutant strain of Streptococcus faecalis.
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Autolysis↗
Inhibition of bacterial cell wall mucopeptide synthesis: a new function of RNA bacteriophage Qbeta.
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Amino Acids↗
Lysis of halophilic Vibrio alginolyticus and Vibrio costicolus induced by chaotropic anions.
High concentration (1.0 M) of KSCN, but not of NaSCN, induced lysis of slightly halophilic Vibrio alginolyticus and moderately halophilic Vibrio costicolus, and the decrease in absorbance of the cell suspension was complete after 30 min at 25 degrees C. Replacement of K+ with Na+ effectively prevented the lysis by SCN-.K+ salts of NO3-, Br- and I-, however, induced no significant lysis. In electron micrographs, a prolonged exposure of the cells of V. alginolyticus to 1.0 M KSCN displaced the nucleoplasm to maintain close contact with the cell membranes. After 40 min of interaction, 50% of the cellular protein, 96% of RNA and 94% of DNA were recovered in the lysed cells. In contrast to lysis in hypotonic conditions, the lysis induced by KSCN is due mainly to a partial release of protein from the cells. V. costicolus was more susceptible to SCN- than V. alginolyticus, whereas nonhalophilic Escherichia coli was resistant to 1.0 M KSCN. Thus, lysis by SCN- is characteristic of halophilic bacteria and cell membranes of more halophilic bacteria are more susceptible to chaotropic anions. The protective effect of Na+ observed here was considered to be manifested by specific interactions of Na+ with components of cell membranes, thereby rendering their structures resistant to the action of chaotropic anions.
Bacteriolysis↗
Bacteriolytic factor in the salivary glands of Aedes aegypti.
Salivary gland homogenates from adult Aedes aegypti lyse Micrococcus lysodeikticus cells. The bacteriolytic factor is present in a cell type common to both male and female mosquitoes, as well as in the crop of sugar-feeding mosquitoes. The bacteriolytic factor releases digestion products from sacculi of Escherichia coli that are different from those of hen egg white lysozyme.
Aedes↗
Age dependence of salivary bacteriolytic activity in adult mosquitoes.
1. Bacteriolytic activity in the salivary glands of adult Aedes aegypti female mosquitoes starts from a low level upon emergence, increases 6-fold over the first 3 days, then levels off. 2. Mosquitoes start sugar-feeding after 2 days, when lytic activity is one-half of the peak level. 3. Bacteriolytic activity in salivary gland extracts is not influenced by removal of corpora allata.
Aedes↗
Digestion of bacteria and the role of midgut lysozyme in some insect larvae.
1. Lysozyme is absent from tissues other than the midgut in the drug-feeding larvae of Musca domestica (Diptera, Cyclorrhapha, Muscidae) and in the fruit-feeding larvae of Anastrepha fraterculus (Diptera, Cyclorrhapha, Tephritidae), whereas in the detritus-feeding larvae of Trichosia pubescens (Diptera, Nematocera, Sciaridae) lysozyme is only found in the hemolymph and in the fat body. 2. A. fraterculus larvae have a midgut region with a luminal pH of 3.4, and display a pepstatin-inhibited acid proteolytic activity which has a spec. act. (7.2 U/mg protein) similar to that of M. domestica. 3. The midgut lysozyme from M. domestica and A. fraterculus is more active (high ionic strength) at pH 3.5 than at pH 6.0, the contrary being true for a midgut chitinase. 4. The results suggest that the adaptations to digest bacteria in insects are similar to those in vertebrate foregut fermenters, and that these characteristics were probably present in the Cyclorrhapha ancestor, but not in the Diptera ancestor.
Animals↗
A procedure to purify RNA and DNA molecules from Streptomyces coelicolor A3 (2).
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Bacteriolysis↗
Infection of Streptococcus oralis NCTC 11427 by pneumococcal phages.
We have found a group of pneumococcal bacteriophages (Cp-1, Cp-7) that can successfully infect and replicate in Streptococcus oralis, whereas Dp-1 was unable to infect this species. We have also developed conditions that allowed transfection of S. oralis using Dp-1 DNA. Our results support the direct involvement of the phage-coded lysins in the liberation of the phage progeny from infected S. oralis cells. Since S. oralis and S. pneumoniae are bacteria that share the same ecological niche in humans, the availability of the system described here should allow to extend our current studies on the modular organization of the lytic enzymes and might serve as a tool to study the evolutionary relationships between host and parasite.
Bacteriolysis↗
Lower autolytic activity in a homogeneous methicillin-resistant Staphylococcus aureus strain compared to derived heterogeneous-resistant and susceptible strains.
It has been proposed that in addition to production of a penicillin-binding protein with low affinity for beta-lactam antibiotics, control of autolysin activity is involved in the mechanism of staphylococcal methicillin resistance. A homogeneous methicillin-resistant Staphylococcus aureus strain (DU4916) had lower rates of unstimulated, NaCl- and Triton X-100-stimulated autolysis, and daptomycin (LY146032)-induced lysis than a heterogeneous methicillin-resistant strain (DU4916-K7) and a methicillin-susceptible strain (DU4916S) derived from DU4916.
Bacteriolysis↗
Correlation between the effects of fosfomycin and chloramphenicol on Escherichia coli.
It was speculated that the increase of the UDP-GlcNAc pool observed with chloramphenicol can modulate the residual PEP:UDP-GlcNAc-enolpyruvate activity of fosfomycin-treated cells. This provided an explanation on how chloramphenicol can insure the formation of enough UDP-MurNAc-pentapeptide to sustain peptidoglycan synthesis at a rate that will antagonize fosfomycin-induced lysis.
Bacteriolysis↗
Autolysins are direct involved in the bactericidal effect caused by penicillin in wild type and in tolerant pneumococci.
The two pneumococcal autolytic enzymes (an N-acetylmuramoyl-L-alanine amidase and an endo-beta-1,4-N-acetylglucosaminidase) are directly involved in the penicillin-induced killing of Streptococcus pneumoniae. The activity of these lytic enzymes was efficiently controlled in tolerant mutants under physiological conditions.
Acetylglucosaminidase↗
Reconstruction and expression of the autolytic gene from Clostridium acetobutylicum ATCC 824 in Escherichia coli.
The complete lyc gene encoding the autolytic lysozyme of Clostridium acetobutylicum ATCC 824 was reconstructed from two overlapping DNA fragments and cloned into a suitable plasmid enabling Escherichia coli to produce this lytic enzyme under the control of the lac promoter. A polypeptide with an apparent M(r) of 35,000, corresponding to that predicted from the nucleotide sequence, was observed by maxicell analysis of whole-cell extracts of E. coli harboring the clostridial gene. The enzyme yield was shown to depend on the pH of the culture medium, since the protein was unstable at alkaline pH. The expression of the lyc gene was not increased by using the E. coli strong promoter, lpp-lac, probably due to the limit imposed by the extreme differences in codon usage. Although the LYC lysozyme does not contain a cleavable signal peptide, most of the protein was found in the periplasmic fraction of E. coli suggesting that this enzyme was secreted through a specific mechanism, as already observed for other autolysins.
Bacteriolysis↗
Synthesis of two bacteriophage lambda S proteins in an in vivo system.
Bacteriophage lambda has two genes which are essential for lysis: R, a gene encoding a 158-amino-acid (aa) transglycosylase that attacks the peptidoglycan, and S, a gene encoding two inner-membrane-associating proteins, designated S105 and S107 for their predicted lengths in aa residues. S105 and S107 are thought to have opposing roles in lysis, with the former acting as the lethal lysis effector and the latter as a lysis inhibitor. Here, we used a T7-polymerase-mediated expression system to show that S105 and S107 are synthesized at a constant ratio of about 2.5:1 throughout the period leading up to lysis, indicating that lysis scheduling does not require a translationally controlled switch from inhibitor (S107) to effector (S105) synthesis. However, evidence is presented that the mRNA sequences immediately 5' to the ribosome-binding site (RBS) of the S gene are required for the rather limited translation, but not the stability, of the S mRNA. No difference could be found in the pattern of ternary complex formation over the two S start codons in in vitro toe-printing assays with the wild-type mRNA and with mRNA deleted of the upstream sequences. Nevertheless, these results may suggest a role for translational control in S gene expression, if not in its temporal regulation or in the partition between S105 and S107 production.
Amino Acid Sequence↗
Positive-selection vector with enhanced lytic potential based on a variant of phi X174 phage gene E.
A cloning vector, pUH89, allowing positive selection of recombinant Escherichia coli clones by insertional inactivation of the modified lysis gene E of bacteriophage phi X174, was developed. Ten unique cloning sites were introduced into gene E by site-directed mutagenesis. To achieve efficient expression of the mutagenized gene, the combined lac and tac promoters were used. Additional restriction sites in the flanking sequences allow screening for transcription terminators and the excision of several cartridges suitable for vector construction.
Amino Acid Sequence↗
Characterization of an insertion in the phage phi 105 genome that blocks host Bacillus subtilis lysis and provides strong expression of heterologous genes.
A defective prophage vector, phi 105MU331, for high-level protein overproduction in Bacillus subtilis, was derived by random insertion of a lacZ reporter gene. The site of insertion not only provided efficient inducible transcription of heterologous genes, but also prevented lysis of the host cell. The region of the insertion in phi 105MU331 lies close to the right cohesive end of phi 105. DNA sequence analysis revealed that this region of phi 105 somewhat resembles the lysis cassette of various phages, including lambda. The site of insertion lies in a possible 'holin' gene, which could explain the block in host cell lysis. Dual promoters apparently responsible for the strong inducible transcription lie in an untranslated region just upstream from the putative holin gene. This region is probably equivalent to the site of the major late promoter and antiterminator of the lambdoid phages. The sequence features could, thus, account for the useful properties of the phi 105MU331 vector system.
Amino Acid Sequence↗
Purification and peptidase activity of a bacteriolytic extracellular enzyme from Pseudomonas aeruginosa.
A bacteriolytic enzyme excreted by Pseudomonas aeruginosa Paks I was purified: samples were found to be homogeneous by gel filtration chromatography, ion exchange chromatography using CM-cellulose, immunoelectrophoresis, PAGE and SDS-PAGE. The molecular weight of the lytic enzyme was estimated to be 15,000-19,000. The enzyme was active on Gram-positive bacteria with glycine-containing interpeptide bridges in their murein layers. In addition, this lytic enzyme showed peptidase activity catalysing the hydrolysis of pentaglycine peptides into tri- and diglycine peptides.
Bacteriolysis↗
Salt requirements in the denitrifying bacterium Pseudomonas nautica 617.
Pseudomonas nautica 617, which was isolated from superficial marine sediment, was found to require sodium for growth. Growth also appeared to be sensitive to the divalent cation, Mg2+, the presence of which, together with that of Na+, was necessary for achieving maximal growth. We investigated cell capacity to resist lysis after washing with either 0.05 M MgCl2 or 0.5 M NaCl, by monitoring suspension optical density changes as well as the release of ultraviolet absorbing material. Mg2+ turned out to play a significant role in stabilizing the structure of the cell envelope. Respiratory activity was also sensitive to ionic environment. With cells washed with 0.05 M MgCl2 and suspended in 0.05 M Tris buffer, the respiration rate, assessed by N2O evolution, was 15% of that measured in artificial sea water. Upon addition of 0.5 M Na+, nitrous oxide production rose to 32% of the reference level. The dinitrification rate was fully restored by further addition of 0.05 M Mg2+. K+ alone had almost no effect, but when added with Na+, the rate of denitrification increased to 45%.
Bacteriolysis↗