TAILIEUCHUNG - Báo cáo khoa học: On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomes

High-resolution crystal structures of large ribosomal subunits from Deinococcus radioduranscomplexed with tRNA-mimics indicate that precise substrate positioning, mandatory for efficient protein biosynthesis with no further conformational rearrangements, is governed by remote interactions of the tRNA helical features. Based on the peptidyl transferase center (PTC) architecture, on the placement of tRNA mimics, and on the existence of a two-fold related region consisting of about 180 nucleotides of the 23S RNA, we proposed a unified mechanism integra-ting peptide bond formation, A-to-P site translocation, and the entrance of the nascent protein into its exit tunnel. . | Eur. J. Biochem. 270 2543-2556 2003 FEBS 2003 doi THE EMBO LECTURE On peptide bond formation translocation nascent protein progression and the regulatory properties of ribosomes Delivered on 20 October 2002 at the 28th FEBS Meeting in Istanbul Ilana Agmon1 Tamar Auerbach1 2 David Baram1 Heike Bartels3 Anat Bashan1. Rita Berisio3 Paola Fucini4 Harly A. S. Hansen3 Joerg Harms3 Maggie Kessler1 Moshe Peretz1 Frank Schluenzen3 Ada Yonath1 3 and Raz Zarivach1 1Department of Structural Biology The Weizmann Institute Rehovot Israel 2FB Biologie Chemie Pharmazie Frei University Berlin Germany 3Max Planck Research Unit for Ribosomal Structure Hamburg Germany 4Max Planck Institute for Molecular Genetics Berlin Germany High-resolution crystal structures of large ribosomal subunits from Demococcus radiodurans complexed with tRNA-mimics indicate that precise substrate positioning mandatory for efficient protein biosynthesis with no further conformational rearrangements is governed by remote interactions of the tRNA helical features. Based on the peptidyl transferase center PTC architecture on the placement of tRNA mimics and on the existence of a twofold related region consisting of about 180 nucleotides of the 23S RNA we proposed a unified mechanism integrating peptide bond formation A-to-P site translocation and the entrance of the nascent protein into its exit tunnel. This mechanism implies sovereign albeit correlated motions of the tRNA termini and includes a spiral rotation of the A-site tRNA-3 end around a local two-fold rotation axis identified within the PTC. PTC features ensuring the precise orientation required for the A-site nucleophilic attack on the P-site carbonyl-carbon guide these motions. Solvent mediated hydrogen transfer appears to facilitate peptide bond formation in conjunction with the spiral rotation. The detection of similar two-fold symmetry-related regions in all known structures of the large ribosomal subunit indicate .

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