核糖体肽出口通道入口处一个保守的氯霉素结合位点。
A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel.
作者信息
Long Katherine S, Porse Bo T
机构信息
Department of Biological Chemistry, Institute of Molecular Biology, University of Copenhagen, Sølvgade 83H, DK-1307 Copenhagen K, Denmark.
出版信息
Nucleic Acids Res. 2003 Dec 15;31(24):7208-15. doi: 10.1093/nar/gkg945.
Abstract
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.
摘要
抗生素氯霉素与大肠杆菌和嗜盐嗜盐菌的核糖体结合并经365nm光照后，会使23S rRNA发生修饰。这些修饰分别定位在大肠杆菌23S rRNA的结构域II和V中的核苷酸m(5)U747和C2611/C2612，以及嗜盐嗜盐菌23S rRNA结构域V中的G2084（按大肠杆菌编号为2058）。修饰位点与大环内酯结合位点的一部分重叠，并聚集在肽出口通道的入口处。这些数据与最近报道的古细菌核糖体上的氯霉素结合位点相关，并表明大肠杆菌核糖体上存在类似的结合位点。
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