Unraveling the Function of Bacterial-Type Phosphoenolpyruvate Carboxylase in Vascular Plants

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dc.contributor.authorTing, Michaelen
dc.contributor.departmentBiologyen
dc.contributor.supervisorPlaxton, William C.en
dc.date2016-09-29 20:09:46.997
dc.date.accessioned2016-10-03T18:47:00Z
dc.date.issued2016-10-03
dc.degree.grantorQueen's University at Kingstonen
dc.descriptionThesis (Master, Biology) -- Queen's University, 2016-09-29 20:09:46.997en
dc.description.abstractTwo distinct phosphoenolpyruvate carboxylase (PEPC) isozymes occur in vascular plants and green algae: plant-type PEPC (PTPC) and bacterial-type PEPC (BTPC). PTPC polypeptides typically form a tightly regulated cytosolic Class-1 PEPC homotetramer. BTPCs, however, appear to be less widely expressed and to exist only as catalytic and regulatory subunits that physically interact with co-expressed PTPC subunits to form hetero-octameric Class-2 PEPC complexes that are highly desensitized to Class-1 PEPC allosteric effectors. Yeast two-hybrid studies indicated that castor plant BTPC (RcPPC4) interacts with all three Arabidopsis thaliana PTPC isozymes, and that it forms stronger interactions with AtPPC2 and AtPPC3, suggesting that specific PTPCs are preferred for Class-2 PEPC formation. In contrast, Arabidopsis BTPC (AtPPC4) appeared to interact very weakly with AtPPC2 and AtPPC3, suggesting that BTPCs from different species may have different physical properties, hypothesized to be due to sequence dissimilarities within their ~10 kDa intrinsically disordered region. Recent RNA-seq and microarray data were analyzed to obtain a better understanding of BTPC expression patterns in different tissues of various monocot and dicot species. High levels of BTPC transcripts, polypeptides and Class-2 PEPC complexes were originally discovered in developing castor seeds, but the analysis revealed a broad range of diverse tissues where abundant BTPC transcripts are also expressed, such as the developing fruits of cucumber, grape, and tomato. Marked BTPC expression correlated well with the presence of ~116 kDa immunoreactive BTPC polypeptides, as well as Class-2 PEPC complexes in the immature fruit of cucumbers and tomatoes. It is therefore hypothesized that in vascular plants BTPC and thus Class-2 PEPC complexes maintain anaplerotic PEP flux in tissues with elevated malate levels that would potently inhibit ‘housekeeping’ Class-1 PEPCs. Elevated levels of malate can be used by biosynthetically active sink tissues such as immature tomatoes and cucumbers for rapid cell expansion, drought or salt stressed roots for osmoregulation, and developing seeds and pollen as a precursor for storage lipid and protein biosynthesis.en
dc.description.degreeM.Sc.en
dc.description.restricted-thesisThesis chapters are in preparation for journal submission. I would like to keep it restricted for 6 months.en
dc.embargo.liftdate2017-11-07
dc.embargo.terms1825en
dc.identifier.urihttp://hdl.handle.net/1974/15042
dc.language.isoengen
dc.relation.ispartofseriesCanadian thesesen
dc.rightsQueen's University's Thesis/Dissertation Non-Exclusive License for Deposit to QSpace and Library and Archives Canadaen
dc.rightsProQuest PhD and Master's Theses International Dissemination Agreementen
dc.rightsIntellectual Property Guidelines at Queen's Universityen
dc.rightsCopying and Preserving Your Thesisen
dc.rightsThis publication is made available by the authority of the copyright owner solely for the purpose of private study and research and may not be copied or reproduced except as permitted by the copyright laws without written authority from the copyright owner.en
dc.subjectPlant Metabolismen
dc.subjectPlant Biochemistryen
dc.subjectPEPCen
dc.subjectPhosphoenolpyruvateen
dc.titleUnraveling the Function of Bacterial-Type Phosphoenolpyruvate Carboxylase in Vascular Plantsen
dc.typethesisen
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