Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu.
Deacylated tRNA is released from the E site upon A site occupation but before GTP is hydrolyzed by EF-Tu.
复制标题
在部位职业时,在EF-TU水解GTP之前,从E部位释放了脱酰化的tRNA。
DOI:
10.1093/nar/gki833
复制
发表时间:
2005
影响因子:
14.9
通讯作者:
Nierhaus, KH
中科院分区:
文献类型:
--
作者:
Dinos, G;Kalpaxis, DL;Wilson, DN;Nierhaus, KH
The presence or absence of deacylated tRNA at the E site sharply influences the activation energy required for binding of a ternary complex to the ribosomal A site indicating the different conformations that the E-tRNA imparts on the ribosome. Here we address two questions: (i) whether or not peptidyltransferase—the essential catalytic activity of the large ribosomal subunit—also depends on the occupancy state of the E site and (ii) at what stage the E-tRNA is released during an elongation cycle. Kinetics of the puromycin reaction on various functional states of the ribosome indicate that the A-site substrate of the peptidyltransferase center, puromycin, requires the same activation energy for peptide-bond formation under all conditions tested. We further demonstrate that deacylated tRNA is released from the E site by binding a ternary complex aminoacyl-tRNA•EF-Tu•GDPNP to the A site. This observation indicates that the E-tRNA is released after the decoding step but before both GTP hydrolysis by EF-Tu and accommodation of the A-tRNA. Collectively these results reveal that the reciprocal linkage between the E and A sites affects the decoding center on the 30S subunit, but does not influence the rate of peptide-bond formation at the active center of the 50S subunit.
登录
查看更多内容
影响因子:
2.9
作者:
FAHNESTOCK, S;NEUMANN, H;RICH, A
通讯作者:
RICH, A
影响因子:
4.8
作者:
Robert, F;Brakier-Gingras, L
通讯作者:
Brakier-Gingras, L
影响因子:
16
作者:
Dinos, G;Wilson, DN;Nierhaus, KH
通讯作者:
Nierhaus, KH
影响因子:
2.9
作者:
NIERHAUS, KH
通讯作者:
NIERHAUS, KH
DOI:
10.1073/pnas.93.22.12183
发表时间:
1996-10-29
影响因子:
11.1
作者:
Semenkov, YP;Rodnina, MV;Wintermeyer, W
通讯作者:
Wintermeyer, W