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. 2013 Nov 8;42(3):2049–2063. doi: 10.1093/nar/gkt1107

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© The Author(s) 2013. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — rpL10 loop mutants inversely affect ligand binding to the A- and P-sites. (a–c) Steady state binding of indicated ligands for ribosomes. (a) Dissociation constants obtained from assays of binding of Ac-aa-tRNA to the P-site, aa-tRNA to the A-site and eEF2 to ribosomes isolated from cells expressing wild-type rpL10 and the rpL10-S104D and rpL10-A106R mutants. (b) Titration of eEF1A into aa-tRNA binding reactions similar to (a). (c) Dissociation constants obtained from assays of binding of Sdo1p to indicated ribosomes. (d) Competition assays. Binding of aa-Phe-tRNA^Phe or Ac-Phe-tRNA^Phe at half maximal concentrations was monitored in the presence of increasing amounts of Sdo1p. Peptidyltransferase activity was similarly monitored. Bars indicate SEM (n = 4 for a, b, n = 3 for c), *P < 0.05, **P < 0.01 (compared to wild type unless noted).