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Biomedical subjects

E Cundliffe

Publications and source records attributed to E Cundliffe.

At least 91 records · Page 5Linked to original sources
PubMed1979

Requirement for ribosomal protein BM-L11 in stringent control of RNA synthesis in Bacillus megaterium.

A spontaneously occurring thiostrepton-resistant mutant of Bacillus megaterium has been shown to yield ribosomes lacking protein BM-L11, a protein immunologically related to Escherichia coli ribosomal protein L11. Here we have demonstrated that the mutant strain has acquired the relaxed phenotype and is unable to synthesise guanosine tetraphosphate and pentaphosphate in vivo. Ribosomes from the mutant strain are unable to support the synthesis of these two compounds in vitro, but this deficiency can be overcome by re-addition of purified protein BM-L11 to the ribosomes. Thus protein BM-L11 appears to be indispensable for the synthesis of guanosine tetraphosphate and pentaphosphate; the implications of this observation are discussed.

Anti-Bacterial Agents↗
PubMed1979

Methylation of basic proteins in ribosomes from wild-type and thiostrepton-resistant strains of Bacillus megaterium and their electrophoretic analysis.

Ribosomes, radioactively labelled in vivo with both [1-14C]methionine and [methyl-3H]methionine, have been isolated from both wild-type and thiostrepton-resistant strains of Bacillus megaterium and their constituent proteins separated by two-dimensional gel electrophoresis. Ribosomes from the wild-type strain possess one basic protein that is extensively methylated. In contrast no such protein can be detected in ribosomes from the thiostrepton-resistant strain.

Anti-Bacterial Agents↗
PubMed1979

Binding of thiostrepton to a complex of 23-S rRNA with ribosomal protein L11.

Thiostrepton binds with high affinity and with a 1 : 1 stoichiometry to a complex formed between Escherichia coli 23-S ribosomal RNA and ribosomal protein L11 of E. coli or the homologous protein BM-L11 of Bacillus megaterium. In the presence of T1 ribonuclease, protein BM-L11 and thiostrepton protect from degradation a fragment of E. coli 23-S RNA estimated to be about 50 nucleotides in length.

Anti-Bacterial Agents↗
PubMed1979

Effects of apramycin, a novel aminoglycoside antibiotic on bacterial protein synthesis.

1. The novel aminoglycoside antibiotic apramycin is shown to be a potent inhibitor of protein synthesis in bacteria both in vivo and in vitro. 2. In cell-free systems from Escherichia coli programmed with poly(U), apramycin induces translation errors, as assayed by incorporation of leucine, isoleucine and serine, although this effect occurs only to a limited extent. 3. Apramycin inhibits the translocation step of protein synthesis both in vivo, in protoplasts of Bacillus megaterium, and in vitro, in cell-free systems from E. coli. It is proposed that this is the primary inhibitory effect of the drug.

Anti-Bacterial Agents↗
PubMed1978

The mode of action of alpha sarcin and a novel assay of the puromycin reaction.

A new technique was developed for measuring the amount of peptidyl-tRNA in a protein-synthesizing system in vitro. By this technique the course of the puromycin reaction may be followed and the modes of action of various inhibitors of protein synthesis readily determined. We conclude that the polypeptide alpha sarcin inhibits the binding of aminoacyl-tRNA into the ribosomal 'A' site, that sparsomycin inhibits the peptidyl transferase reaction and that cycloheximide may block translocation.

Animals↗
PubMed1977

Inhibition of initiation, elongation, and termination of eukaryotic protein synthesis by trichothecene fungal toxins.

The 12,13-epoxytrichothecenes, specific inhibitors of protein synthesis in eukaryotes, can be subdivided further in terms of their mode of action. In addition to the I-type (initiation inhibitors) and E-types (elongation inhibitors), we found that some E-types apparently exhibit inhibition of chain termination at low concentrations. The nature of substituents on C4 may determine the type of inhibitory activity observed.

Centrifugation, Density Gradient↗
PubMed1975

Properties of the ribosomes of antibiotic producers: effects thiostrepton and micrococcin on the organisms which produce them.

Ribosomes of Streptomyces azureus, which produces thiostrepton, are resistant to thiostrepton by virtue of being unable to bind the antibiotic. These ribosomes are also resistant to a number of other antibiotics (the thiostrepton group) which may share a common ribosomal binding site and a common mode of action with thiostrepton. Conversely, Bacillus pumilis and a strain of micrococcus, which produce the (probably identical) antibiotics micrococcin P and micrococcin, respectively, possess ribosomes which are susceptible to these antibiotics in vitro, although the organisms themselves are resistant.

Anti-Bacterial Agents↗
PubMed1975

Inhibition of ribosomal A site functions by sporangiomycin and micrococcin.

Sporangiomycin and micrococcin inhibit the binding of aminoacyl-transfer ribonucleic acid into the ribosomal A site in intact bacterial protoplasts. They also prevent the assembly of [ribosome-elongation factor G-guanine nucleotide] complexes in vitro and compete with [(35)S]thiostrepton for ribosomal binding sites. We conclude that micrococcin and sporangiomycin block the ribosomal A site in the vicinity of the complex guanosine triphosphatase center and so resemble thiostrepton in their modes of action.

Anti-Bacterial Agents↗
PubMed1974

Mechanism of inhibition of eukaryotic protein synthesis by trichothecene fungal toxins.

The 12,13-epoxytrichothecenes, a group of sesquiterpenoid fungal antibiotics, inhibit protein synthesis in eukaryotic cells but do not share a common mode of action. Trichodermin stabilizes polyribosomes, prevents their disaggregation by puromycin, and also prevents the release of nascent peptides from ribosomes by puromycin. Nivalenol, T-2 toxin, and verrucarin A cause rapid and almost quantitative breakdown of polyribosomes in H-HeLa cells, a process which is inhibited by anisomycin, cycloheximide, or trichodermin. Similar effects of trichodermin, nivalenol, and verrucarin A are also observed in yeast spheroplasts. We conclude that nivalenol, T-2 toxin, and verrucarin A are potent and highly selective inhibitors of polypeptide chain initiation in eukaryotes, whereas trichodermin inhibits chain elongation and (or) termination. We have compared the structural formulae of various trichothecenes and suggest that the presence of substituents on carbon-15 of the common trichothecene ring may be important in determining the precise modes of action of this group of compounds.

Acremonium↗
PubMed1972

Some unique properties of the deoxyribonucleic acid-bearing portion of the bacterial membrane.

By using the M-band technique we have shown that portions of the membranes of Bacillus megaterium and Escherichia coli vary in their affinity for magnesium-Sarkosyl crystals and in phospholipid composition. The portion to which deoxyribonucleic acid is attached comprises as little as 4% of the total cell membrane, has a particularly high degree of affinity for magnesium-Sarkosyl crystals, and is rich in phosphatidylethanolamine. The M-band fractionation does not depend on the use of lysozyme.

Bacillus megaterium↗