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oai:www.ideals.illinois.edu:2142/87049 2023-07-11 col_2142_5131 col_2142_16357 com_2142_5130 com_2142_16356 com_2142_8913 com_2142_8903

Archie R. Portis, Jr. Li, Cishan 2015-09-28T15:22:54Z 2015-09-28T15:22:54Z 10000-01-01 2006 2006 Heat sensitivity of Rubisco activase(s) confers a major limitation on leaf photosynthesis at moderately high temperature in Arabidopsis. To overcome this limitation, a thermostable activase for Arabidopsis was generated by engineering the more thermostable tobacco activase with an Arabidopsis Rubisco recognition domain. The resulting chimeric activase displayed an improved thermostability, activated Arabidopsis Rubisco and maintained Rubisco activation state at moderately high temperature in vitro. Transgenic Arabidopsis plants expressing the chimeric activase were created, allowing for further characterization. Made available in DSpace on 2015-09-28T15:22:54Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3223653.pdf: 2218022 bytes, checksum: d521eac89e440c0a447eaf1d1e940554 (MD5) Previous issue date: 2006 Embargo set by: Seth Robbins for item 88330 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 92 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006. http://hdl.handle.net/2142/87049 (MiAaPQ)AAI3223653 eng Chemistry, Biochemistry Identifying the Rubisco Recognition Domain and Critical Arginines in Activase and Engineering Activase With Improved Thermostability for Arabidopsis text Plant Biology Plant Biology University of Illinois at Urbana-Champaign Dissertation Ph.D.