Structural and functional studies of birnavirus RNA polymerases---Insights into the protein-priming mechanism and the evolution of RNA viruses

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dc.contributor.advisorTao, Yizhi Janeen_US
dc.creatorPan, Junhuaen_US
dc.date.accessioned2009-06-03T19:52:14Zen_US
dc.date.available2009-06-03T19:52:14Zen_US
dc.date.issued2008en_US
dc.description.abstractThe first crystal structure of a birnavirus polymerase, IBDV VP1, has been determined at 2.5 A resolution by multiple isomorphous replacement and anomalous scattering (MIR-AS). The VP1 structure reveals several highly unusual features. By adopting a novel topology in the polymerase palm subdomain, VP1 is able to bring several functional motifs into spatial proximity to form a complete polymerase active site, despite the permutaion of sequence. By modeling initiation and elongation complexes onto the VP1 structure, important structural features are demonstrated and insights into the functions of the birnavirus self-guanylylation and protein-primed RNA synthesis are presented. Both self-guanylylation and nucleotide polymerization activities of VP1 are explored using various biochemical approaches; and based on the combination these findings and site-directed mutagenesis, speculations about the mechanisms of the self-guanylylation active site and the unusual polymerase active site are presented. Moreover, the VP1 structure lends further support for the evolutionary relationship between dsRNA and +ssRNA viruses. Progress in crystallographic and functional studies on other birnavirus polymerases and various functional complexes are also provided for the future direction of further investigation on the structural basis of the protein-priming mechanism by birnavirus VP1.en_US
dc.format.extent248 p.en_US
dc.format.mimetypeapplication/pdfen_US
dc.identifier.callnoTHESIS BIOCHEM. 2008 PANen_US
dc.identifier.citationPan, Junhua. "Structural and functional studies of birnavirus RNA polymerases---Insights into the protein-priming mechanism and the evolution of RNA viruses." (2008) Diss., Rice University. <a href="https://hdl.handle.net/1911/22170">https://hdl.handle.net/1911/22170</a>.en_US
dc.identifier.urihttps://hdl.handle.net/1911/22170en_US
dc.language.isoengen_US
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.subjectMicrobiologyen_US
dc.subjectBiochemistryen_US
dc.subjectBiophysicsen_US
dc.titleStructural and functional studies of birnavirus RNA polymerases---Insights into the protein-priming mechanism and the evolution of RNA virusesen_US
dc.typeThesisen_US
dc.type.materialTexten_US
thesis.degree.departmentBiochemistry and Cell Biologyen_US
thesis.degree.disciplineNatural Sciencesen_US
thesis.degree.grantorRice Universityen_US
thesis.degree.levelDoctoralen_US
thesis.degree.nameDoctor of Philosophyen_US
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