Probing the Role of Highly Conserved Lysine (K279) Residue in the Editing Domain of Bacterial Prolyl-tRNA Synthetases

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dc.contributor.advisorBhattacharyya, Sudeep
dc.contributor.advisorHati, Sanchita
dc.contributor.authorMueller, Irene C.
dc.contributor.authorCao, Bach
dc.contributor.authorMeitzner, Karl J.
dc.contributor.authorTschudy, Matthew J.
dc.date.accessioned2011-11-10T20:09:17Z
dc.date.available2011-11-10T20:09:17Z
dc.date.issued2011-05
dc.descriptionColor poster with text, diagrams, charts, and graphs.en
dc.description.abstractThe Escherichia coli (Ec) prolyl-tRNA synthetase enzyme possesses three distinct domains. One of the domains, the editing domain, is critical for proofreading the charged tRNAPro, ensuring the correct amino acid has been attached to the tRNA molecule. In this editing domain, a highly conserved lysine has been found to be absolutely essential for proofreading. Through site-directed mutagenesis and enzyme kinetic studies this study attempted to probe the role of this lysine residue (K279).en
dc.description.sponsorshipUniversity of Wisconsin--Eau Claire Office of Research and Sponsored Programs; NIH-AREA granten
dc.identifier.urihttp://digital.library.wisc.edu/1793/55083
dc.language.isoen_USen
dc.relation.ispartofseriesUSGZE AS589en
dc.subjectCatalytic RNAen
dc.subjectFunctional analysisen
dc.subjectEscherichia coli
dc.subjectLysineen
dc.subjectPostersen
dc.subjectLigasesen
dc.subjectMicrobiological synthesisen
dc.titleProbing the Role of Highly Conserved Lysine (K279) Residue in the Editing Domain of Bacterial Prolyl-tRNA Synthetasesen
dc.typePresentationen

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