Chimeras of bacterial translation factors Tet(O) and EF-G.
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.
Thakor
Nehal S
NS
Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.
Nechifor
Roxana
R
Scott
Paul G
PG
Keelan
Monika
M
Taylor
Diane E
DE
Wilson
Kevin S
KS
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D015153:Blotting, Western; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D008958:Models, Molecular; D020653:Peptide Elongation Factor G / Q000737:chemistry / Q000235:genetics*; D014176:Protein Biosynthesis; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D020653:Peptide Elongation Factor G; D011993:Recombinant Fusion Proteins; C083139:Tet O resistance protein, Bacteria