Toward understanding the function of the universally conserved GTPase HflX

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dc.contributor.authorFischer, Jeffrey J.
dc.contributor.supervisorWieden, Hans-Joachim
dc.contributor.supervisorBoeré, René T.
dc.date.accessioned2013-11-29T19:22:01Z
dc.date.available2013-11-29T19:22:01Z
dc.date.issued2011
dc.degree.levelPhD
dc.descriptionxii, 185 leaves : ill. (some col.) ; 28 cmen_US
dc.description.abstractMembers 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.identifier.urihttps://hdl.handle.net/10133/3313
dc.language.isoen_CAen_US
dc.publisherLethbridge, Alta. : University of Lethbridge, Dept. of Chemistry and Biochemistry, c2011en_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.subjectGuanosine triphosphataseen_US
dc.subjectGuanosine triphosphatase -- Researchen_US
dc.subjectProteins -- Synthesisen_US
dc.titleToward understanding the function of the universally conserved GTPase HflXen_US
dc.typeThesisen_US
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