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Mechanism and Rates of Exchange of L7/L12 between Ribosomes and the Effects of Binding EF-G

Deroo, Stephanie (författare)
Hyung, Suk-Joon (författare)
Marcoux, Julien (författare)
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Gordiyenko, Yuliya (författare)
Koripella, Ravi Kiran (författare)
Uppsala universitet,Struktur- och molekylärbiologi
Sanyal, Suparna (författare)
Uppsala universitet,Struktur- och molekylärbiologi
Robinson, Carol V. (författare)
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 (creator_code:org_t)
2012-04-18
2012
Engelska.
Ingår i: ACS Chemical Biology. - : American Chemical Society (ACS). - 1554-8929 .- 1554-8937. ; 7:6, s. 1120-1127
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • The ribosomal stalk complex binds and recruits translation factors to the ribosome during protein biosynthesis. In Escherichia coli the stalk is composed of protein L10 and four copies of L7/L12. Despite the crucial role of the stalk, mechanistic details of L7/L12 subunit exchange are not established. By incubating isotopically labeled intact ribosomes with their unlabeled counterparts we monitored the exchange of the labile stalk proteins by recording mass spectra as a function of time. On the basis of kinetic analysis, we proposed a mechanism whereby exchange proceeds via L7/L12 monomers and dimers. We also compared exchange of L7/L12 from free ribosomes with exchange from ribosomes in complex with elongation factor G (EF-G), trapped in the posttranslocational state by fusidic acid. Results showed that binding of EF-G reduces the L7/L12 exchange reaction of monomers by similar to 27% and of dimers by similar to 47% compared with exchange from free ribosomes. This is consistent with a model in which binding of EF-G does not modify interactions between the L7/L12 monomers but rather one of the four monomers, and as a result one of the two dimers, become anchored to the ribosome-EF-G complex preventing their free exchange. Overall therefore our results not only provide mechanistic insight into the exchange of L7/L12 monomers and dimers and the effects of EF-G binding but also have implications for modulating stability in response to environmental and functional stimuli within the cell.

Ämnesord

NATURVETENSKAP  -- Biologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences (hsv//eng)

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