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.
Original language | English |
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Pages (from-to) | 20-26 |
Number of pages | 7 |
Journal | FEBS Letters |
Volume | 567 |
Issue number | 1 |
DOIs | |
State | Published - 1 Jun 2004 |
Externally published | Yes |
Keywords
- Antibiotics synergism
- Azithromycin
- Dual binding
- Peptide-bond formation
- Positional catalysis
- Ribosome
- Synercid
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology