A base pair between tRNA and 235 rRNA in the peptidyl transferase centre of the ribosome

Nature ◽  
1995 ◽  
Vol 378 (6555) ◽  
pp. 419-419 ◽  
Author(s):  
Raymond R. Samaha ◽  
Rachel Green ◽  
Harry F. Noller
Nature ◽  
1995 ◽  
Vol 377 (6547) ◽  
pp. 309-314 ◽  
Author(s):  
Raymond R. Samaha ◽  
Rachel Green ◽  
Harry F. Noller

1997 ◽  
Vol 4 (10) ◽  
pp. 775-778 ◽  
Author(s):  
Elisabetta Viani Puglisi ◽  
Rachel Green ◽  
Harry F. Noller ◽  
Joseph D. Puglisi

1982 ◽  
Vol 7 (11) ◽  
pp. 385-386 ◽  
Author(s):  
R.A. Garrett ◽  
Paul Wooley

2005 ◽  
Vol 33 (3) ◽  
pp. 488-492 ◽  
Author(s):  
A. Bashan ◽  
A. Yonath

A ribosome is a ribozyme polymerizing amino acids, exploiting positional- and substrate-mediated chemical catalysis. We showed that peptide-bond formation is facilitated by the ribosomal architectural frame, provided by a sizable symmetry-related region in and around the peptidyl transferase centre, suggesting that the ribosomal active site was evolved by gene fusion. Mobility in tunnel components is exploited for elongation arrest as well as for trafficking nascent proteins into the folding space bordered by the bacterial chaperone, namely the trigger factor.


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