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Chimeras of bacterial translation factors Tet(O) and EF‐G
Author(s) -
Thakor Nehal S.,
Nechifor Roxana,
Scott Paul G.,
Keelan Monika,
Taylor Diane E.,
Wilson Kevin S.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.03.023
Subject(s) - elongation factor , ribosome , biology , escherichia coli , protein biosynthesis , ribosomal rna , fusion protein , ribosomal protein , campylobacter jejuni , tetracycline , biochemistry , bacteria , rna , recombinant dna , genetics , antibiotics , gene
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.