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A Role for the 2' OH of peptidyl-tRNA substrate in peptide release on the ribosome revealed through RF-mediated rescue
Johns Hopkins University School of Medicine, Baltimore.
Institutionen för Cell och Molekylärbiologi, Uppsala Universitet.ORCID iD: 0000-0002-0468-9664
Johns Hopkins University School of Medicine, Baltimore.
Institutionen för Cell och Molekylärbiologi, Uppsala Universitet.
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2012 (English)In: Chemistry and Biology, ISSN 1074-5521, E-ISSN 1879-1301, Vol. 19, no 8, p. 983-993Article in journal (Refereed) Published
Abstract [en]

The 2' OH of the peptidyl-tRNA substrate is thought to be important for catalysis of both peptide bond formation and peptide release in the ribosomal active site. The release reaction also specifically depends on a release factor protein (RF) to hydrolyze the ester linkage of the peptidyl-tRNA upon recognition of stop codons in the A site. Here, we demonstrate that certain amino acid substitutions (in particular those containing hydroxyl or thiol groups) in the conserved GGQ glutamine of release factor RF1 can rescue defects in the release reaction associated with peptidyl-tRNA substrates lacking a 2' OH. We explored this rescue effect through biochemical and computational approaches that support a model where the 2' OH of the P-site substrate is critical for orienting the nucleophile in a hydrogen-bonding network productive for catalysis.

Place, publisher, year, edition, pages
2012. Vol. 19, no 8, p. 983-993
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Theoretical Chemistry
Identifiers
URN: urn:nbn:se:hkr:diva-12006DOI: 10.1016/j.chembiol.2012.06.011ISI: 000309152500010PubMedID: 22921065OAI: oai:DiVA.org:hkr-12006DiVA: diva2:719826
Available from: 2014-05-27 Created: 2014-05-27 Last updated: 2017-12-05Bibliographically approved

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Trobro, Stefan

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