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  Ribosome-induced tuning of GTP hydrolysis by a translational GTPase.

Maracci, C., Peske, F., Dannies, E., Pohl, C., & Rodnina, M. V. (2014). Ribosome-induced tuning of GTP hydrolysis by a translational GTPase. Proceedings of the National Academy of Sciences of the United States of America, 111(40), 14418-14423. doi: 10.1073/pnas.1412676111.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0023-EE46-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-80E8-8
Genre: Journal Article

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Maracci, C.1, Author              
Peske, F.1, Author              
Dannies, E., Author
Pohl, C.1, Author              
Rodnina, M. V.1, Author              
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1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

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 Abstract: GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in decoding and translational fidelity. The basic reaction mechanism and the way the ribosome contributes to catalysis are a matter of debate. Here we use mutational analysis in combination with measurements of rate/pH profiles, kinetic solvent isotope effects, and ion dependence of GTP hydrolysis by EF-Tu off and on the ribosome to dissect the reaction mechanism. Our data suggest that—contrary to current models—the reaction in free EF-Tu follows a pathway that does not involve the critical residue H84 in the switch II region. Binding to the ribosome without a cognate codon in the A site has little effect on the GTPase mechanism. In contrast, upon cognate codon recognition, the ribosome induces a rearrangement of EF-Tu that renders GTP hydrolysis sensitive to mutations of Asp21 and His84 and insensitive to K+ ions. We suggest that Asp21 and His84 provide a network of interactions that stabilize the positions of the γ-phosphate and the nucleophilic water, respectively, and thus play an indirect catalytic role in the GTPase mechanism on the ribosome.

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Language(s): eng - English
 Dates: 2014-09-222014-10-07
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1412676111
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Title: Proceedings of the National Academy of Sciences of the United States of America
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Source Genre: Journal
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Pages: - Volume / Issue: 111 (40) Sequence Number: - Start / End Page: 14418 - 14423 Identifier: -