Visualizing tmRNA entry into a stalled ribosome

被引：120

作者：

Valle, M

Gillet, R

Kaur, S

Henne, A

Ramakrishnan, V

Frank, J

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

[2] Hlth Res Inc, Wadsworth Ctr, Howard Hughes Med Inst, Albany, NY 12201 USA

[3] Inst Microbiol & Genet, Gottingen Genom Lab, D-37077 Gottingen, Germany

[4] SUNY Albany, Dept Biomed Sci, Albany, NY 12201 USA

来源：

SCIENCE | 2003年 / 300卷 / 5616期

关键词：

D O I：

10.1126/science.1081798

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：

Bacterial ribosomes stalled on defective messenger RNAs (mRNAs) are rescued by tmRNA, an similar to300-nucleotide-long molecule that functions as both transfer RNA (tRNA) and mRNA. Translation then switches from the defective message to a short open reading frame on tmRNA that tags the defective nascent peptide chain for degradation. However, the mechanism by which tmRNA can enter and move through the ribosome is unknown. We present a cryo-electron microscopy study at similar to13 to 15 angstroms of the entry of tmRNA into the ribosome. The structure reveals how tmRNA could move through the ribosome despite its complicated topology and also suggests roles for proteins S1 and SmpB in the function of tmRNA.

引用

页码：127 / 130

页数：5

共 38 条

[1] Kinetic parameters for tmRNA binding to alanyl-tRNA synthetase and elongation factor Tu from Escherichia coli [J].