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• W2000798648 abstract "During translation elongation, the ribosome compositional factors elongation factor G (EF-G; encoded by fusA) and tRNA alternately bind to the ribosome to direct protein synthesis and regulate the conformation of the ribosome. Here, we use single-molecule fluorescence with zero-mode waveguides to directly correlate ribosome conformation and composition during multiple rounds of elongation at high factor concentrations in Escherichia coli. Our results show that EF-G bound to GTP (EF-G-GTP) continuously samples both rotational states of the ribosome, binding with higher affinity to the rotated state. Upon successful accommodation into the rotated ribosome, the EF-G-ribosome complex evolves through several rate-limiting conformational changes and the hydrolysis of GTP, which results in a transition back to the nonrotated state and in turn drives translocation and facilitates release of both EF-G-GDP and E-site tRNA. These experiments highlight the power of tracking single-molecule conformation and composition simultaneously in real time." @default.
• W2000798648 created "2016-06-24" @default.
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• W2000798648 date "2013-04-28" @default.
• W2000798648 modified "2023-10-18" @default.
• W2000798648 title "Coordinated conformational and compositional dynamics drive ribosome translocation" @default.
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• W2000798648 doi "https://doi.org/10.1038/nsmb.2567" @default.
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