RNA Chaperone Activity of the RRM2 Domain of Human La

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dc.contributor.advisorBayfield, Mark
dc.creatorSharifi, Samel
dc.date.accessioned2015-12-16T19:29:28Z
dc.date.available2015-12-16T19:29:28Z
dc.date.copyright2015-08-26
dc.date.issued2015-12-16
dc.date.updated2015-12-16T19:29:28Z
dc.degree.disciplineBiology
dc.degree.levelMaster's
dc.degree.nameMSc - Master of Science
dc.description.abstractGenuine La proteins are abundant RNA binding factors that primarily facilitate maturation of nascent precursor RNAs in eukaryotes. Chaperone activity is a conserved feature in the La superfamily, yet the structural basis for this activity remains obscure. RNAs bound by human La (hLa) primarily make contacts with the conserved La module in the N-terminal domain. However, a role for the non- canonical RRM2 fold in the C-terminal domain (CTD) has been proposed recently. Using gel shift assays, nuclear magnetic resonance (NMR) spectroscopy, and circular dichroism (CD) spectroscopy, we aim to understand hLa’s uncharacterized RRM2 dependent binding. Our results demonstrate that the RRM2 relies on non-canonical features including a subsequent disordered C terminal to bind RNA. Consequently, we predict that this region becomes ordered to facilitate hLa’s chaperone function. Taken together, these data support a model for disordered regions in chaperone activity and expand our understanding of La’s function.
dc.identifier.urihttp://hdl.handle.net/10315/30736
dc.language.isoen
dc.rightsAuthor owns copyright, except where explicitly noted. Please contact the author directly with licensing requests.
dc.subjectMolecular biology
dc.subjectBiochemistry
dc.subjectCellular biology
dc.subject.keywordsRNA chaperone
dc.subject.keywordsRNA remodelling
dc.subject.keywordsLa protein
dc.subject.keywordsLupus autoantigen
dc.subject.keywordsRNA recognition motif
dc.subject.keywordsRRM2
dc.subject.keywordsLa human
dc.subject.keywordsentropy transfer
dc.titleRNA Chaperone Activity of the RRM2 Domain of Human La
dc.typeElectronic Thesis or Dissertation

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