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Biomedical subjects

A Bollen

Publications and source records attributed to A Bollen.

At least 163 records · Page 9Linked to original sources
PubMed1980

Polarity of amber mutations in ribosomal protein genes of Escherichia coli.

Two amber mutations have been mapped inside the spcA-strA region (now called rpsE-rpsL) on the bacterial genome. Derivatives of the transducing phage lambda fus3 carrying each mutation were constructed and assayed in ultraviolet-irradiated bacteria to identify the mutated genes and measure the polarity of the mutations. The data indicated that both mutations, 3162(Am) and 3161(Am), affect genes coding for ribosomal proteins: rplC (L3) and rpsN (S14), respectively. It was shown also that each mutation exerts, inside of its respective operon (S10 and spc units), a relatively strong polar effect on genes distal to the mutated locus.

Bacterial Proteins↗
PubMed1979

A missense mutation in the gene coding for ribosomal protein S17 (rpsQ) leading to ribosomal assembly defectivity in Escherichia coli.

The conditionally lethal mutation, 2861 mis, has been mapped inside the ribosomal protein gene cluster at 72 minutes on the Escherichia coli chromosome and was found to cotransduce at 97% with rpsE (S5). The 2861 mis mutation leads to thermosensitivity and impaired assembly in vivo of 30S ribosomal particles at 42 degrees C. The strain carrying the mutation has an altered S 17 ribosomal protein; the mutational alteration involves a replacement of serine by phenylalanine in protein S 17. Spontaneous reversion to temperature independence can restore the normal assembly in vivo of 30 S ribosomal subunits at 42 degrees C and the normal chromatographical behaviour of the S 17 ribosomal protein in vitro. We conclude therefore that the 2861 mis mutation affects the structural gene for protein S 17 (rpsQ).

Bacterial Proteins↗
PubMed1978

Resistance to the aminoglycoside antibiotic neamine in Escherichia coli. A new mutant whose NeaR phenotype results from the cumulative effects of two distinct mutations.

A spontaneous mutant of Escherichia coli (strain AB2847), selected for resistance to the aminoglycoside antibiotic neamine, shows severe restriction of amber suppressors in vivo. Ribosomes isolated from the mutant exhibit only low misreading in vitro in the presence of the antibiotic. Genetic and biochemical analyses indicate that the neamine-resistant phenotype is the result of two distinct mutations. The first, res3128, appears to affect the gene (strA) coding for the ribosomal protein S12. Although it leads to a restrictive phenotype it does not, however, confer resistance to streptomycin. The second mutation, X3128, is located between the sirA and AROB loci and is lethal when segregated from the res3128 mutation. It may affect the ribosome at the level of a post-translational modification.

Drug Resistance, Microbial↗
PubMed1978

Phage Mu-1 mediated transposition: a tool to study the organization of ribosomal protein genes in Escherichia coli.

Phage Mu-1 mediated transposition has been used to map genes coding for ribosomal proteins and elongation factor G inside transcriptional units. The data indicate that 1) the str A and fusA genes belong to the same operon, 2) the spcA and strA genes are expressed independently, 3) the spcA gene is located in a different transcriptional unit to that of the eryA and eryB genes.

Coliphages↗
PubMed1977

Amber mutations in Escherichia coli essential genes: isolation of mutants affected in the ribosomes.

A method to obtain amber mutations in ribosomal protein genes is described. tit relies on the P1-mediated localized mutagenesis (Hong and Ames, 1971) and on the fact that the recipient strain contains (a) an efficient but genetically unstable suppressor, (b) a particular thermoinducible lambda prophage which kills suppressor hosts at 42 degrees C. Exposure of these bacteria to the high temperature yields frequent suppressor-free derivatives while none will be found if the strain carries an amber mutation in an essential gene. Eleven mutants have been isolated by this method, of which at least six appear to carry amber mutations. All of them map close to, and to the right of spcA, in a region which codes mostly for ribosomal proteins. Three mutants were studied biochemically; all three show defective ribosomal assembly in vivo upon loss of suppression.

Bacteriological Techniques↗
PubMed1977

A new nucleic acid-protein cross-linking reagent.

A new photoactivable reagent is described, which allows the formation of RNA-protein cross-links via disulfide bridges in combination with mercaptobutyrimidate. The reconstituted L24 protein-23S RNA complex from the large subunit of E. coli ribosomes has been used as a model system for the cross-linking. The main advantages of the reagent are the absence of U.V. generated cross-links, since photoactivation is carried out at 360 nm, on one hand and the ease of cleavage of the cross-link by mild reduction (beta-mercaptoethanol) on the other.

Diazonium Compounds↗
PubMed1977

Translational fidelity in Escherichia coli: contrasting role of neaA and ramA gene products in the ribosome functioning.

Strains carrying both the ramA1 and the neaA301 mutations do not exhibit the restriction of informational suppressors normally associated with resistance to neamine. Furthermore, ribosomes from such strains exhibit increased misreading in vitro with respect to particles from the neaA strain. These properties suggest that translational fidelity may be cooperatively controlled by ribosomal proteins S4 and S17, coded by ramA (rpsd) and neaA (rpsq) genes respectively.

Drug Resistance, Microbial↗
PubMed1976

Cooperative control of translational fidelity by ribosomal proteins in Escherichia coli. III. A ram mutation in the structural gene for protein S5 (rpx E).

The effect on translational fidelity of a particular mutation in the gene coding for protein S5(rpxE) has been investigated. This mutation has the opposite effect of a restrictive strA mutation; in vivo, it relieves the restriction imposed by strA on the suppression of T4 nonsense mutants and results in hypersensitivity to streptomycin; in vitro, the presence of the altered S5 protein in 30S ribosomes results in increased intrinsic misreading. It is concluded that this mutation, ramC319, acts as a ribosomal ambiguity mutation similar to certain mutations of protein S4 (ramA).

Bacterial Proteins↗