Modulating the activity of the peptidyl transferase center of the ribosome

被引:19
作者
Beringer, Malte [1 ,2 ]
机构
[1] Ctr Gen Regulat, Barcelona 08003, Spain
[2] Univ Witten Herdecke, Inst Phys Biochem, D-58448 Witten, Germany
关键词
ribosome; peptidyl transferase center; peptide bond formation; peptide release; SecM; TnaC;
D O I
10.1261/rna.980308
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The peptidyl transferase (PT) center of the ribosome catalyzes two nucleophilic reactions, peptide bond formation between aminoacylated tRNA substrates and, together with release factor, peptide release. Structure and function of the PT center are modulated by binding of aminoacyl-tRNA or release factor, thus providing the basis for the specificity of catalysis. Another way by which the function of the PT center is controlled is signaling from the peptide exit tunnel. The SecM nascent peptide induces ribosome stalling, presumably by inhibition of peptide bond formation. Similarly, the release factor-induced hydrolytic activity of the PT center can be suppressed by the TnaC nascent peptide contained in the exit tunnel. Thus, local and long-range conformational rearrangements can lead to changes in the reaction specificity and catalytic activity of the PT center.
引用
收藏
页码:795 / 801
页数:7
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