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Biomedical subjects

A Kaji

Publications and source records attributed to A Kaji.

At least 145 records · Page 8Linked to original sources
PubMed1974

Molecular nature of the deoxyribonucleic acid of a thermosensitive R factor, Rts1.

The deoxyribonucleic acid of the thermosensitive R factor, Rts1, has been examined by the technique of sedimentation in alkaline sucrose, electron microscopy, and radiation target size. All these methods yielded a molecular weight of approximately 120 million for Rts1 deoxyribonucleic acid in Escherichia coli. Sedimentation analysis revealed that Rts1 deoxyribonucleic acid in Proteus mirabilis was also 120 million daltons. Rts1 did not segregate into E. coli minicells under the conditions where another smaller non-thermosensitive R factor could.

Centrifugation, Density Gradient↗
PubMed1973

Host cell growth in the presence of the thermosensitive drug resistance factor, Rts1.

We have confirmed and extended the observation of Terawaki et al. that the R factor, Rts1, alters the growth of its host at 42 C. In all media tested there was a period during which total cell numbers increased linearly, while viable counts remained constant. During this period the rate of precursor incorporation per cell particle into deoxyribonucleic acid, ribonucleic acid, and protein declined steadily. These patterns were a consequence of the accumulation of increasing numbers of cells which had lost colony-forming ability. A temperature shiftdown experiment showed that the colony formers could, after a lag, go on to divide normally, whereas most of the noncolony formers could not undergo even a limited number of divisions after shiftdown. The number of normal divisions which occurred after shiftup of Rts1 cells to 42 C was medium dependent. In rich medium there were, on the average, two or three doublings; in glucose medium, one; and in glycerol medium, only a fraction of a doubling. Even in glucose medium, however, no increase in viable counts was observed during growth at 42 C if the cells were first starved for glucose for 1 h at 42 C. A temperature shiftdown from 42 C to 27 C during glucose starvation reversed the effect of starvation at 42 C alone. These results are consistent with the hypothesis that the thermosensitive Rts1 component(s) responsible for the host effects is present at permissive temperature, but can undergo a reversible temperature-induced alteration which then interferes with some essential host function. The detrimental effects of this R factor on its host were also reflected in a heightened sensitivity to kanamycin and actinomycin D at 42 C. Electron microscope observations revealed changes in the appearance of the cell membrane. Membranous invaginations were noted at discrete sites in the cell.

Bacterial Proteins↗
PubMed1972

Evidence for specific inhibition of translocation of aminoacyl-transfer ribonucleic acid by the pretreatment of ribosomes of Bacillus subtilis with p-chloromercuribenzoate.

The biological activities of Bacillus subtilis ribosomes pretreated with 0.5, 1, or 2 mmp-chloromercuribenzoate (PCMB) were examined. The ribosomes treated with 1 or 2 mm PCMB lost their capacity to synthesize polyphenylalanine as well as the capacity to bind phenylalanyl-transfer ribonucleic acid. On the other hand, approximately 70% of the polyphenylalanine synthesis capacity was lost with ribosomes pretreated with 0.5 mm PCMB. This inhibition was found to be due to a specific inhibition of the translocation step. The effect of 0.5 mm PCMB was reversed by 20 mm Mg(2+) without the loss of PCMB bound to ribosomes, while beta-mercaptoethanol partially reversed the inhibitory effect with concomitant loss of bound PCMB.

Bacillus subtilis↗
PubMed1972

Effect of bacteriophage ghost infection on protein synthesis in Escherichia coli.

The rate of protein synthesis by Escherichia coli markedly decreased within 1 min after phage T4 infection, whereas a complete cessation of protein synthesis was observed within at least 25 sec after T4 ghost infection. The cellular level of amino acids and aminoacyl-transfer ribonucleic acid (tRNA) did not change drastically upon infection with ghosts, indicating that the inhibition of protein synthesis took place at a step(s) beyond aminoacyl-tRNA formation. The host messenger RNA remained intact and still bound to ribosomes shortly after ghost infection. Kinetic studies of the effect of ghosts on host protein synthesis revealed that nascent peptide chains on ribosomes were not released upon ghost infection.

Amino Acids↗