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dc.identifier.urihttp://hdl.handle.net/11401/76905
dc.description.sponsorshipThis work is sponsored by the Stony Brook University Graduate School in compliance with the requirements for completion of degree.en_US
dc.formatMonograph
dc.format.mediumElectronic Resourceen_US
dc.language.isoen_US
dc.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dc.typeThesis
dcterms.abstractPost-transcriptional trafficking of mRNA within the cell provides for spatial regulation of protein expression. Cis-acting localization elements known as zip codes located often in 3' untranslated regions (UTRs) of mRNA transcripts play a strong role in directing distribution within the cell through recognition by RNA-binding proteins. Hnrnpab is a protein with putative roles in this process with RNA-binding properties likely directed through tandem RNA Recognition Motifs (RRMs) that form a cooperative RNA Binding Domain (RBD). We purified this Hnrnpab RBD and carried out electrophoretic mobility shift assays (EMSAs) using the zip code region from the ActB gene to demonstrate high specificity binding. In order to determine the structural determinants of this specificity we purified and 13C, 15N-labeled Hnrnpab RBD for analysis by solution NMR to begin determining a structure for the RRMs both with and without high specificity RNA partners. Further characterization of how Hnrnpab recognizes its targets and what structural motifs determine this type of binding will facilitate greater understanding of the spatial regulation of protein products necessary for cellular and organismal development.
dcterms.available2017-09-20T16:51:25Z
dcterms.contributorSmith, Steven.en_US
dcterms.contributorCzaplinski, Kevinen_US
dcterms.creatorCatt, Daniel
dcterms.dateAccepted2017-09-20T16:51:25Z
dcterms.dateSubmitted2017-09-20T16:51:25Z
dcterms.descriptionDepartment of Biochemistry and Cell Biology.en_US
dcterms.extent34 pg.en_US
dcterms.formatApplication/PDFen_US
dcterms.formatMonograph
dcterms.identifierhttp://hdl.handle.net/11401/76905
dcterms.issued2013-12-01
dcterms.languageen_US
dcterms.provenanceMade available in DSpace on 2017-09-20T16:51:25Z (GMT). No. of bitstreams: 1 Catt_grad.sunysb_0771M_11681.pdf: 3438653 bytes, checksum: be165413f1c08a2fbbfc830ec716afdf (MD5) Previous issue date: 1en
dcterms.publisherThe Graduate School, Stony Brook University: Stony Brook, NY.
dcterms.subjectBiochemistry
dcterms.subjectEMSA, Hnrnpab, NMR, RRM
dcterms.titleStructural and Biochemical Analysis of the Hnrnpab Tandem RRM RNA Binding Domain
dcterms.typeThesis


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