A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel.
The antibiotic chloramphenicol produces modifications in 23S rRNA when bound to ribosomes from the bacterium Escherichia coli and the archaeon Halobacterium halobium and irradiated with 365 nm light. The modifications map to nucleotides m(5)U747 and C2611/C2612, in domains II and V, respectively, of E.coli 23S rRNA and G2084 (2058 in E.coli numbering) in domain V of H.halobium 23S rRNA. The modification sites overlap with a portion of the macrolide binding site and cluster at the entrance to the peptide exit tunnel. The data correlate with the recently reported chloramphenicol binding site on an archaeal ribosome and suggest that a similar binding site is present on the E.coli ribosome.
Long
Katherine S
KS
Department of Biological Chemistry, Institute of Molecular Biology, University of Copenhagen, Sølvgade 83H, DK-1307 Copenhagen K, Denmark. long@mermaid.molbio.ku.dk
Porse
Bo T
BT
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001483:Base Sequence; D001665:Binding Sites; D002701:Chloramphenicol / Q000378:metabolism* / Q000494:pharmacology; D004926:Escherichia coli / Q000235:genetics*; D019617:Halobacterium salinarum / Q000235:genetics*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D010455:Peptides / Q000378:metabolism*; D014176:Protein Biosynthesis; D012338:RNA, Ribosomal, 23S / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects; D016914:Ribonuclease H / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000235:genetics / Q000378:metabolism* / Q000528:radiation effects; D014466:Ultraviolet Rays
D000900:Anti-Bacterial Agents; D010455:Peptides; D012338:RNA, Ribosomal, 23S; D002701:Chloramphenicol; D016914:Ribonuclease H