{"id":{"repo_id":"wustl","oai_identifier":"oai:openscholarship.wustl.edu:etd-1885"},"canonical_url":"https://search.dev.ndltd.org/etd/wustl/oai:openscholarship.wustl.edu:etd-1885","repository":{"repo_id":"wustl","name":"Washington University in St. Louis","base_url":"https://openscholarship.wustl.edu/do/oai/"},"display":{"title":"Genetic and Biochemical Properties of Arabidopsis RNA Polymerases IV and V","abstract":"RNA Polymerases IV and V: Pol IV and Pol V) are plant-specific enzyme complexes with subunit homology to RNA Polymerase II: Pol II). The largest subunits in Pol IV and Pol V, NRPD1 and NRPE1 respectively, share a second largest subunit, NRPD2/NRPE2. The evolutionarily conserved Metal A and Metal B binding sites are required for Pol IV and V in vivo function fitting the prediction that these are functional polymerases. The Defective Chloroplast and Leaves-like: DeCL) domain at the C-terminus of both NRPD1 and NRPE1 is also required for complementation but other domains in the NRPE1 CTD are largely dispensable. Biochemical analysis reveals Pol IV to be a DNA-dependent RNA Polymerase capable of producing RNA from a tripartite template that mimics an open transcription bubble. The Metal A binding site is required for Pol IV in vitro transcription while the enzyme is resistant to alpha-amanitin, a potent Pol II inhibitor. Pol IV has also been found to physically associate with RNA DEPENDENT RNA POLYMERASE 2: RDR2) in vivo providing an explanation for how Pol IV RNA products are channeled specifically to RDR2 for the production of double-stranded RNA and eventual dicing. Biochemical analysis has also revealed that RDR2 is capable of transcribing both single-stranded RNA and DNA in vitro, consistent with previously analyzed RNA-dependent RNA polymerases from plants and other organisms.","abstract_html":"RNA Polymerases IV and V: Pol IV and Pol V) are plant-specific enzyme complexes with subunit homology to RNA Polymerase II: Pol II). The largest subunits in Pol IV and Pol V, NRPD1 and NRPE1 respectively, share a second largest subunit, NRPD2/NRPE2. The evolutionarily conserved Metal A and Metal B binding sites are required for Pol IV and V in vivo function fitting the prediction that these are functional polymerases. The Defective Chloroplast and Leaves-like: DeCL) domain at the C-terminus of both NRPD1 and NRPE1 is also required for complementation but other domains in the NRPE1 CTD are largely dispensable. Biochemical analysis reveals Pol IV to be a DNA-dependent RNA Polymerase capable of producing RNA from a tripartite template that mimics an open transcription bubble. The Metal A binding site is required for Pol IV in vitro transcription while the enzyme is resistant to alpha-amanitin, a potent Pol II inhibitor. Pol IV has also been found to physically associate with RNA DEPENDENT RNA POLYMERASE 2: RDR2) in vivo providing an explanation for how Pol IV RNA products are channeled specifically to RDR2 for the production of double-stranded RNA and eventual dicing. Biochemical analysis has also revealed that RDR2 is capable of transcribing both single-stranded RNA and DNA in vitro, consistent with previously analyzed RNA-dependent RNA polymerases from plants and other organisms.","abstract_has_math":false,"creators":["Haag, Jeremy"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biology and Biomedical Sciences: Plant and Microbial Biosciences","degree_department":null,"school":null,"contributors":["Craig Pikaard"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2009,"date_issued":"2009-05-24T07:00:00Z","date_published":"2009-05-24T07:00:00Z","updated_at":"2026-07-24T06:12:58Z","subjects":["Biology","Molecular","Pol IV","Pol V","RDR2","RNA polymerase","RNA-directed DNA methylation","Transcription"],"languages":["English (en)"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.7936/K7Z60M2B"],"render_values":[{"text":"https://doi.org/10.7936/K7Z60M2B","href":"https://doi.org/10.7936/K7Z60M2B","code":true}]}]},"links":{"outbound_url":"https://openscholarship.wustl.edu/etd/886","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Craig Pikaard"]},{"key":"dc:creator","label":"Author","values":["Haag, Jeremy"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2013-05-25T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology and Biomedical Sciences: Plant and Microbial Biosciences"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biology","Molecular","Pol IV","Pol V","RDR2","RNA polymerase","RNA-directed DNA methylation","Transcription"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["English (en)"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://openscholarship.wustl.edu/etd/886"]},{"key":"dc:identifier.doi","label":"DOI","values":["https://doi.org/10.7936/K7Z60M2B"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["RNA Polymerases IV and V: Pol IV and Pol V) are plant-specific enzyme complexes with subunit homology to RNA Polymerase II: Pol II). The largest subunits in Pol IV and Pol V, NRPD1 and NRPE1 respectively, share a second largest subunit, NRPD2/NRPE2. The evolutionarily conserved Metal A and Metal B binding sites are required for Pol IV and V in vivo function fitting the prediction that these are functional polymerases. The Defective Chloroplast and Leaves-like: DeCL) domain at the C-terminus of both NRPD1 and NRPE1 is also required for complementation but other domains in the NRPE1 CTD are largely dispensable. Biochemical analysis reveals Pol IV to be a DNA-dependent RNA Polymerase capable of producing RNA from a tripartite template that mimics an open transcription bubble. The Metal A binding site is required for Pol IV in vitro transcription while the enzyme is resistant to alpha-amanitin, a potent Pol II inhibitor. Pol IV has also been found to physically associate with RNA DEPENDENT RNA POLYMERASE 2: RDR2) in vivo providing an explanation for how Pol IV RNA products are channeled specifically to RDR2 for the production of double-stranded RNA and eventual dicing. Biochemical analysis has also revealed that RDR2 is capable of transcribing both single-stranded RNA and DNA in vitro, consistent with previously analyzed RNA-dependent RNA polymerases from plants and other organisms."]},{"key":"dc:title","label":"Title","values":["Genetic and Biochemical Properties of Arabidopsis RNA Polymerases IV and V"]}]}],"canonical_facts":{"dc:contributor":["Craig Pikaard"],"dc:creator":["Haag, Jeremy"],"dc:date.available":["2013-05-25T07:00:00Z"],"dc:description.abstract":["RNA Polymerases IV and V: Pol IV and Pol V) are plant-specific enzyme complexes with subunit homology to RNA Polymerase II: Pol II). The largest subunits in Pol IV and Pol V, NRPD1 and NRPE1 respectively, share a second largest subunit, NRPD2/NRPE2. The evolutionarily conserved Metal A and Metal B binding sites are required for Pol IV and V in vivo function fitting the prediction that these are functional polymerases. The Defective Chloroplast and Leaves-like: DeCL) domain at the C-terminus of both NRPD1 and NRPE1 is also required for complementation but other domains in the NRPE1 CTD are largely dispensable. Biochemical analysis reveals Pol IV to be a DNA-dependent RNA Polymerase capable of producing RNA from a tripartite template that mimics an open transcription bubble. The Metal A binding site is required for Pol IV in vitro transcription while the enzyme is resistant to alpha-amanitin, a potent Pol II inhibitor. Pol IV has also been found to physically associate with RNA DEPENDENT RNA POLYMERASE 2: RDR2) in vivo providing an explanation for how Pol IV RNA products are channeled specifically to RDR2 for the production of double-stranded RNA and eventual dicing. Biochemical analysis has also revealed that RDR2 is capable of transcribing both single-stranded RNA and DNA in vitro, consistent with previously analyzed RNA-dependent RNA polymerases from plants and other organisms."],"dc:identifier":["https://openscholarship.wustl.edu/etd/886"],"dc:identifier.doi":["https://doi.org/10.7936/K7Z60M2B"],"dc:language":["English (en)"],"dc:subject":["Biology","Molecular","Pol IV","Pol V","RDR2","RNA polymerase","RNA-directed DNA methylation","Transcription"],"dc:title":["Genetic and Biochemical Properties of Arabidopsis RNA Polymerases IV and V"],"thesis:degree_discipline":["Biology and Biomedical Sciences: Plant and Microbial Biosciences"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Doctor of Philosophy (PhD)"]},"updated_at":"2026-07-24T06:12:58Z"}