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Papers In Press, published online ahead of print January 30, 2001
J. Biol. Chem, 10.1074/jbc.M008430200
Submitted on September 14, 2000
Revised on January 30, 2001
Accepted on January 30, 2001
Molecular & Medical Pharmacology, UCLA School of Medicine, Los Angeles, CA 90095-1770
Corresponding Author: pstewart{at}mednet.ucla.edu
The Escherichia coli ribosomal protein L7/L12 is central to the translocation step of translation and it is known to be flexible under some conditions. Assignment of electron density to L7/L12 was not possible in the recent 2.4 Å resolution x-ray crystallographic structure (Ban, N., Nissen, P., Hansen, J., Moore, P. B., and Steitz, T. A. (2000) Science 289, 905-920). We have localized the two dimers of L7/L12 within the structure of the 70S ribosome using two reconstitution approaches together with cryo-electron microscopy and single particle reconstruction. First, structures were determined for ribosomal cores, from which protein L7/L12 had been removed by treatment with NH4Cl and ethanol, and for reconstituted ribosomes, in which purified L7/L12 had been restored to core particles. Difference mapping revealed that the reconstituted ribosomes had additional density within the L7/L12 shoulder next to protein L11. Second, ribosomes were reconstituted using an L7/L12 variant in which a single cysteine at position 89 in the C-terminal domain was modified with Nanogold, a 14 Å gold derivative. Reconstruction from cryo-EM images and difference mapping placed the gold at four interfacial positions. The finding of multiple sites for the C-terminal domain of L7/L12 suggests that the conformation of this protein may change during the steps of elongation and translocation.
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