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- W2012138448 abstract "Whereas considerable information is available on ribosome structure and function, far less is known on how ribosomes are assembled. Our work focuses on a region of the large subunit that binds a number of proteins including L20, an early assembly protein that is essential for the binding of several other r-proteins. On the secondary structure of 23S rRNA this region appears as a long irregular stem, with L20 bound to the bottom. Like for many other ribosomal proteins, the effect of this binding on the structure of the target RNA is not known. By unwinding this region, using a single molecule trapping assay, we localize the L20 binding site within less than two base pairs and we show that L20 increases the stability of the bottom of the stem. Thus L20 acts as a clamp stabilizing the subdomain for later assembly steps. Our approach, which is the first study of this kind on RNA-protein interaction, should be applicable to other RNA-protein complexes." @default.
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- W2012138448 date "2010-01-01" @default.
- W2012138448 modified "2023-09-25" @default.
- W2012138448 title "Mechanical Stabilisation of an Essential Subdomain of the Ribosome" @default.
- W2012138448 doi "https://doi.org/10.1016/j.bpj.2009.12.2546" @default.
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