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dc.contributor.supervisor Wieden, Hans-Joachim
dc.contributor.supervisor Boeré, René T.
dc.contributor.author Fischer, Jeffrey J.
dc.date.accessioned 2013-11-29T19:22:01Z
dc.date.available 2013-11-29T19:22:01Z
dc.date.issued 2011
dc.identifier.uri https://hdl.handle.net/10133/3313
dc.description xii, 185 leaves : ill. (some col.) ; 28 cm en_US
dc.description.abstract Members of the ubiquitous GTPase superfamily regulate numerous cellular functions. A core group of eight GTPases are present in all domains of life: initiation factor 2, elongation factors Tu and G, protein secretion factors Ffh and FtsY, and the poorly characterized factors YihA, YchF, and HflX. While the first five members have well defined roles in the essential cellular process of protein synthesis, a role for YihA, YchF and HflX in this process has only recently been suggested. Here, a detailed kinetic analysis examining the interaction between HflX and its cellular partners is described. 50S and 70S ribosomal particles function as GTPase activating factors for HflX by stabilizing the nucleotide binding pocket of HflX, inducing a “GTPase activated” state. These data indicates a novel mode of GTPase activation, and suggests a role for HflX in regulating translation. en_US
dc.language.iso en_CA en_US
dc.publisher Lethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2011 en_US
dc.subject Guanosine triphosphatase en_US
dc.subject Guanosine triphosphatase -- Research en_US
dc.subject Proteins -- Synthesis en_US
dc.title Toward understanding the function of the universally conserved GTPase HflX en_US
dc.type Thesis en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.degree.level PhD


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