核糖体催化肽键形成，其中A位点底物与23S核糖体RNA共价连接。
Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA.
作者信息
Green R, Switzer C, Noller H F
机构信息
Center for Molecular Biology of RNA, Sinsheimer Laboratories, University of California, Santa Cruz, CA 95064, USA.
出版信息
Science. 1998 Apr 10;280(5361):286-9. doi: 10.1126/science.280.5361.286.
In the ribosome, the aminoacyl-transfer RNA (tRNA) analog 4-thio-dT-p-C-p-puromycin crosslinks photochemically with G2553 of 23S ribosomal RNA (rRNA). This covalently linked substrate reacts with a peptidyl-tRNA analog to form a peptide bond in a peptidyl transferase-catalyzed reaction. This result places the conserved 2555 loop of 23S rRNA at the peptidyl transferase A site and suggests that peptide bond formation can occur uncoupled from movement of the A-site tRNA. Crosslink formation depends on occupancy of the P site by a tRNA carrying an intact CCA acceptor end, indicating that peptidyl-tRNA, directly or indirectly, helps to create the peptidyl transferase A site.
在核糖体中，氨酰基转移RNA（tRNA）类似物4-硫代-dT-p-C-p-嘌呤霉素与23S核糖体RNA（rRNA）的G2553发生光化学交联。这种共价连接的底物与肽基-tRNA类似物反应，在肽基转移酶催化的反应中形成肽键。这一结果将23S rRNA保守的2555环置于肽基转移酶A位点，并表明肽键形成可以独立于A位点tRNA的移动而发生。交联的形成取决于携带完整CCA受体末端的tRNA对P位点的占据，这表明肽基-tRNA直接或间接地有助于形成肽基转移酶A位点。
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