Three tRNAs on the ribosome slow translation elongation

Choi Junhong; Puglisi Joseph D.

首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America. >Three tRNAs on the ribosome slow translation elongation

【24h】

Three tRNAs on the ribosome slow translation elongation

机译：Three tRNAs on the ribosome slow translation elongation

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相关主题

摘要

During protein synthesis, the ribosome simultaneously binds up to three different transfer RNA (tRNA) molecules. Among the three tRNA binding sites, the regulatory role of the exit (E) site, where deacylated tRNA spontaneously dissociates from the translational complex, has remained elusive. Here we use two donor-quencher pairs to observe and correlate both the conformation of ribosomes and tRNAs as well as tRNA occupancy. Our results reveal a partially rotated state of the ribosome wherein all three tRNA sites are occupied during translation elongation. The appearance and lifetime of this state depend on the E-site tRNA dissociation kinetics, which may vary among tRNA species and depends on temperature and ionic strength. The 3-tRNA partially rotated state is not a proper substrate for elongation factor G (EF-G), thus inhibiting translocation until the E-site tRNA dissociates. Our result presents two parallel kinetic pathways during translation elongation, underscoring the ability of E-site codons to modulate the dynamics of protein synthesis.

著录项

来源
《Proceedings of the National Academy of Sciences of the United States of America.》 |2017年第52期|13691-13696|共6页
作者
Choi Junhong; Puglisi Joseph D.;
展开▼
作者单位

Stanford Univ, Dept Appl Phys, Stanford, CA 94305 USA;

Stanford Univ, Sch Med, Dept Biol Struct, Stanford, CA 94305 USA;

展开▼
收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
ribosome; protein synthesis; single-molecule FRET; nonfluorescent quencher; E site;

Three tRNAs on the ribosome slow translation elongation

摘要

著录项

相关主题

期刊订阅