Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050251 | FEBS Letters | 2008 | 5 Pages |
Abstract
Ribosomal protection proteins (RPPs) confer bacterial resistance to tetracycline by releasing this antibiotic from ribosomes stalled in protein synthesis. RPPs share structural similarity to elongation factor G (EF-G), which promotes ribosomal translocation during normal protein synthesis. We constructed and functionally characterized chimeric proteins of Campylobacter jejuni Tet(O), the best characterized RPP, and Escherichia coli EF-G. A distinctly conserved loop sequence at the tip of domain 4 is required for both factor-specific functions. Domains 3–5: (i) are necessary, but not sufficient, for functional specificity; and (ii) modulate GTP hydrolysis by EF-G, while minimally affecting Tet(O), under substrate turnover conditions.
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Authors
Nehal S. Thakor, Roxana Nechifor, Paul G. Scott, Monika Keelan, Diane E. Taylor, Kevin S. Wilson,