Studies on the accessibility of nascent non-helical peptide chains on the ribosome
Evers, U.; Gewitz, H.S.
Biochemistry International 19(5): 1031-1038
1989
ISSN/ISBN: 0158-5231 PMID: 2699792 Document Number: 338813
The accessibility of nascent polypeptides with special structural elements to the ribosome was investigated. Poly(C), poly(C, U) and poly(C, A) mRNAs were translated by E. coli ribosomes in vitro. The resulting peptides which were rich in prolines, remained on the ribosomal particles or were released after addition of puromycin. A protease from Aspergillus oryzae hydrolyzed the released peptides rapidly, whereas the degradation of the unreleased ones was only slightly affected. This result shows that the nascent peptides were protected against proteolytic attack by the ribosomal particles. Interestingly, the protease completely degraded the 30S particles whereas the 50S ones remained intact, even after prolonged incubation.