Ultrastructural investigation of the effect of DNA, RNA, and protein synthesis inhibitors on ribosome crystallization

1973 ◽  
Vol 44 (3-4) ◽  
pp. 265-278 ◽  
Author(s):  
Nadir M. Maraldi ◽  
Graziella Biagini ◽  
Paolo Simoni ◽  
Marcello Barbieri ◽  
Marina Marini ◽  
...  
1974 ◽  
Vol 141 (2) ◽  
pp. 593-595 ◽  
Author(s):  
A. Bhattacharya ◽  
M. Puri ◽  
A. Datta

The presence of N-acetylglucosamine is essential for the induced synthesis of N-acetylglucosamine kinase in Candida albicans. The enzyme synthesis stops and its concentration in the cells declines rapidly as soon as N-acetylglucosamine is removed from the medium. Experiments with RNA- and protein-synthesis inhibitors indicate that the appearance of new enzyme activity is dependent on concomitant new protein synthesis and the inducer operates at a transcriptional level.


1976 ◽  
Vol 21 (2) ◽  
pp. 291-302
Author(s):  
C.J. Flickinger

Amoeba nuclear envelopes were damaged using microsurgery, and metabolic requirements for the steps in their repair were studied, and my placing the cells in a solution containing one of several metabolic inhibitors. The first step in repair, the association of pieces of endoplasmic reticulum with holes in the nuclear membranes, appears to be a passive process since it was not affected by inhibitors of energy production, RNA synthesis, or protein synthesis. In contrast, fusion of pieces of endoplasmic reticulum with the nuclear membranes at the margins of the holes was blocked by KCN and dinitrophenol, indicating that membrane fusion requires energy derived from respiration, but RNA and protein synthesis inhibitors did not prevent fusion of pieces of endoplasmic reticulum with the nuclear membranes. The subsequent completion of repair and restoration of intact nuclear membranes was almost completely blocked by inhibitors of respiration, and it was reduced in the presence of actinomycin and emetine, suggesting that in addition to a requirement for energy, some later steps in the repair of the nuclear membranes require RNA and protein synthesis.


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