SITES OF INTERACTION OF THE CCA END OF PEPTIDYL-TRANSFER RNA WITH 23S RIBOSOMAL-RNA

被引:137
作者
MOAZED, D [1 ]
NOLLER, HF [1 ]
机构
[1] UNIV CALIF SANTA CRUZ, SINSHEIMER LABS, SANTA CRUZ, CA 95064 USA
关键词
RIBOSOMES; PEPTIDYLTRANSFERASE; SPARSOMYCIN;
D O I
10.1073/pnas.88.9.3725
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Oligonucleotide fragments derived from the 3' CCA terminus of acylated tRNA, such as CACCA-(AcPhe), UACCA-(AcLeu), and CAACCA-(fMet), bind specifically to ribosomes in the presence of sparsomycin and methanol [Monro, R. E., Celma, M. L. & Vazquez, D. (1969) Nature (London) 222, 356-358]. All three oligonucleotides protect a characteristic set of bases in 23S rRNA from chemical probes: G2252, G2253, A2439, A2451, U2506, and U2585. A2602 shows enhanced reactivity. These account for most of the same bases that are protected when peptidyl-tRNA analogues such as AcPhe-tRNA are bound to the ribosomal P site, and correspond precisely to those bases whose protection is abolished by removal of the 3'-CA end of tRNA. We conclude that most of the observed interactions between tRNA and 23S rRNA in the 50S ribosomal P site involve the conserved CCA terminus of tRNA. Sparsomycin may inhibit protein synthesis by stabilizing interaction between the peptidyl-CCA and the 23S P site, preventing formation of the intermediate A/P hybrid state.
引用
收藏
页码:3725 / 3728
页数:4
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