| Literature DB >> 15165888 |
Ilana Agmon1, Maya Amit, Tamar Auerbach, Anat Bashan, David Baram, Heike Bartels, Rita Berisio, Inbal Greenberg, Joerg Harms, Harly A S Hansen, Maggie Kessler, Erez Pyetan, Frank Schluenzen, Assa Sittner, Ada Yonath, Raz Zarivach.
Abstract
The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3' end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation.Mesh：
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Year: 2004 PMID： 15165888 DOI： 10.1016/j.febslet.2004.03.065
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124