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Biomedical subjects

R Takata

Publications and source records attributed to R Takata.

At least 37 records · Page 2Linked to original sources
PubMed1985

Attenuation and processing of RNA from the rpsO-pnp transcription unit of Escherichia coli.

Ribosomal protein S15 and polynucleotide phosphorylase of E. coli are encoded by two adjacent genes, rpsO and pnp, respectively. Analysis of in vivo transcripts from these two genes shows that they are within the same operon (S15 operon). By correlating the 5' and 3' ends of their in vivo transcripts with the DNA sequence, we have identified several features of the operon structure. These features include a promotor upstream from rpsO, an attenuator downstream from rpsO and an RNA processing site between these two genes.

Chromosome Mapping↗
PubMed1984

Isolation of a Serratia marcescens mutant which is an efficient recipient for the E. coli episome.

A Serratia marcescens mutant, which is an efficient recipient for the Escherichia coli episome (F' plasmid), was isolated after mutagenesis by N-methyl-N'-nitro-N-nitrosoguanidine (NTG). Episomes could be maintained in the mutant cell under conditions selective for a gene on the plasmid. This S. marcescens mutant could also be transformed with pBR 322 DNA at a frequency higher than that of the parental strain.

Conjugation, Genetic↗
PubMed1984

Nucleotide sequence of the gene for Escherichia coli ribosomal protein S15 (rpsO).

The nucleotide sequence of the ribosomal protein gene rpsO (S15) and its flanking region were determined. The amino acid sequence of S15 protein deduced from the nucleotide sequence is in good agreement with the published amino acid sequence with one exception. The nucleotide sequence shows two probable promoter sites about 100 nucleotides upstream from the initiation codon (AUG) of rpsO. Inspection of the sequence also revealed structural homology between the distal part of rpsO and the reported S15 binding region in 16S rRNA.

Bacterial Proteins↗
PubMed1982

Cloning of rpsO, the gene for ribosomal protein S15 of Escherichia coli.

The gene for Escherichia coli ribosomal protein S15 (rpsO) was cloned on the vector pBR322 from F-prime JCH55 DNA. The recombinant plasmid was transformed to Serratia marcescens cells and it was proved that E. coli S15 was synthesized and incorporated into ribosome particles in S. marcescens cells. A DNA fragment containing rpsO was also inserted into the vector pRF3, which changes its copy number depending on the growth temperature in a temperature-sensitive polA host. By use of this recombinant plasmid it was shown that the relative synthesis rate of S15 increased about twice even when the copy number of the plasmid increased more than twenty-fold.

Cloning, Molecular↗
PubMed1978

The temperature sensitive mutant 72c. I. Pleiotropic growth behaviour and changed response to some antibiotics and mutations in the transcription or translation apparatus.

The spontaneous temperature sensitive mutant 72c is shown to be more tolerant to fusidic acid, but less tolerant to trimethoprim on plates at permissive temperature, than is the parental strain. The poor growth of the mutant on amino acids supplemented plates, as well as its inability to grow on broth plates at 40 degrees, can be compensates by sublethal amounts of chloroamphenicol. Also some mutations to Rif-R or Str-R improve growth of the mutant under certain conditions. Reversion and other genetic analysis strongly suggest, that the pleiotropic behaviour of the mutant is due to a single mutation in a gene, which is designated fusB and is closely cotransducible with lip at min 14 of the E. coli chromosome. The gene order is lip-fusB-supE.

Chloramphenicol↗
PubMed1978

The temperature sensitive mutant 72c. II. Accumulation at high temperature of ppGpp and pppGpp in the presence of protein synthesis.

A heat sensitive mutant of E. coli has been analyzed. A shift to restrictive temperature leads to an accumulation of ppGpp and pppGpp in both the parental and the mutant strains (both are relA+). The pool of these compounds is shown to decrease with time after the temperature shift in the case of the parental strain, but remains at the same elevated level in the case of the mutant. The temperature shift of the mutant leads to an apparent reduction of stable RNA synthesis; this inhibition can be released by chloroamphenicol or tetracycline. Gross protein synthesis is more or less unaffected at restrictive temperature. In the parental strain little effect is seen on RNA and protein synthesis after the temperature shift. A relA derivative of the mutant does not show the same inhibition of RNA synthesis at high temperature. Sedimentation analysis suggests that mutant 70S ribosome are more stable, when exposed to a lowered Mg2+ concentration, than are 70S ribosomes from the parental strain. In addition, the relative amounts of the two forms of ribosomal protein S6, which can be obtained on DEAE chromatography (Held et al., 1973), are significantly changed in the mutant.

Bacterial Proteins↗
PubMed1978

Genetic studies of the ribosomal proteins in Escherichia coli. XI. Mapping of the genes for L21, L27, S15 and S21 by using hybrid bacteria and over-production of these proteins in the merodiploid strains.

E. coli episomes which cover argG region were transferred to S. marcescens and ribosomal proteins (r-proteins) from these hybrid strains were analyzed by two-dimensional (2D) polyacrylamide gel electrophoresis. Three E. coli r-proteins L21, L27 and S15 could be detected in the ribosomes from the hybrid strains. The relative rate of synthesis of the individual r-proteins were determined for E. coli merodiploid strains harboring these episomes. Over-production of three r-proteins L21, L27 and S21 (but not S15) was observed in the merodiploid strains.

Electrophoresis, Polyacrylamide Gel↗
PubMed1977

A procedure for isolation of spontaneous mutants with temperature sensitive of RNA and/or protein.

A procedure for the isolation of spontaneous temperature sensitive mutants of Escherichia coli has been developed. They are selected as survivors at high temperature against the combined killing effects exerted by a temperature inducible lambda prophage and either streptomycin plus ampillicin or ampicillin plus cycloserine. The mutants so obtained are blocked in vivo in the synthesis of RNA or protein or both at restrictive temperature.

Bacterial Proteins↗
PubMed1976

Genetic studies of the ribosomal proteins in Escherichia coli. X. Mapping of the ribosomal proteins, L21 and S15, by intergeneric mating experiments between Serratia marcescens and Escherichia coli K12.

Episomes of E. coli, which cover argG but not the str region, were transferred to Serratia marcescens. Ribosomal proteins from these hybrid strains were analyzed with phospho-cellulose or carboxy-methyl-cellulose column chromatography. Two E. coli ribosomal proteins, L21 and S15, could be detected in the ribosome from the hybrid strains in addition to the ribosomal proteins of S. marcescens.

Bacterial Proteins↗
PubMed1976

Genetic studies of the ribosomal proteins in Escherichia coli. IX. Mapping of the ribosomal proteins, S2 and S20, by intergeneric mating experiments between Serratia marcescens and Escherichia coli K12.

Episomes of E. coli K12, which cover thrleu region of the chromosome, were transferred to Serratia marcescens. Ribosomal proteins from these hybrid strains were analyzed with phosphocellulose column chromatography. Two E. coli 30S ribosomal proteins, S2 and S20, could be detected in the ribosome of the hybrid strain in addition to all ribosomal proteins of S. marcescens.

Chromatography, Ion Exchange↗