Nucleic Acids Research, Vol 26, Issue 4 887-895, Copyright © 1998 by Oxford University Press
KM Choi and R Brimacombe
As part of a programme to investigate the path of the nascent peptide
through the large ribosomal subunit, peptides of different lengths (up to
30 amino acids), corresponding to the signal peptide sequence and N-
terminal region of the Escherichia coli ompA protein, were synthesized in
situ on E.coli ribosomes. The peptides each carried a diazirine moiety
attached to their N-terminus which, after peptide synthesis, was
photoactivated so as to induce cross-links to the 23S rRNA. The results
showed that, with increasing length, the peptides became progressively
cross-linked to sites in Domains V, II, III and I of the 23S rRNA, in a
similar manner to that previously observed with a family of peptides
derived from the tetracycline resistance gene. However, the cross-links to
Domain III appeared at a shorter peptide length (12 aa) in the case of the
ompA sequence, and an additional cross-link in Domain II (localized to nt
780-835) was also observed from this peptide. As with the tetracycline
resistance sequence, peptides of all lengths were still able to form
cross-links from their N-termini to the peptidyl transferase centre in
Domain V. A further set of peptides (30 or 50 aa long), derived from
mutants of the bacteriophage T4 gene 60 sequence, did not show the
cross-links to Domain III, but their N-termini were nevertheless
cross-linked to Domain I and to the sites in Domains II and V. The ability
of relatively long peptides to fold back towards the peptidyl transferase
centre thus appears to be a general phenomenon.
ARTICLES
The path of the growing peptide chain through the 23S rRNA in the 50S ribosomal subunit; a comparative cross-linking study with three different peptide families
Max-Planck-Institut fur Molekulare Genetik, AG-Ribosomen, Ihnestrasse 73, 14195 Berlin, Germany.
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