scholarly journals Caspase-3-dependent and -independent Degradation of 28 S Ribosomal RNA May Be Involved in the Inhibition of Protein Synthesis during Apoptosis Initiated by Death Receptor Engagement

2000 ◽  
Vol 275 (18) ◽  
pp. 13967-13973 ◽  
Author(s):  
Daita Nadano ◽  
Taka-Aki Sato
1994 ◽  
Vol 22 (4) ◽  
pp. 686-693 ◽  
Author(s):  
Sherif Abou Elela ◽  
Liam Good ◽  
Yuri F. Melekhovets ◽  
Ross N. Nazar

1991 ◽  
Vol 15 (1) ◽  
pp. 45-52 ◽  
Author(s):  
Emil H. Nikolov ◽  
Bistra B. Nankova ◽  
Mariana D. Dabeva

1968 ◽  
Vol 36 (1) ◽  
pp. 91-101 ◽  
Author(s):  
R. Soeiro ◽  
M. H. Vaughan ◽  
J. E. Darnell

Inhibition of protein synthesis by puromycin (100 γ/ml) is known to inhibit the synthesis of ribosomes. However, ribosomal precursor RNA (45S) continues to be synthesized, methylated, and processed. Cell fractionation studies revealed that, although the initial processing (45S → 32S + 16S) occurs in the presence of puromycin, the 16S moiety is immediately degraded. No species of ribosomal RNA can be found to have emerged from the nucleolus. The RNA formed in the presence of puromycin is normal as judged by its ability to enter new ribosomal particles after puromycin is removed. This sequence of events is not a result of inhibition of protein synthesis, for cycloheximide, another inhibitor of protein synthesis, either alone or in combination with puromycin allows the completion of new ribosomes.


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