A molecular dissection of the Rubisco activation system from rice

Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) forms inhibited complexes with its own substrate RuBP and other sugar phosphates. The AAA+ protein Rubisco activase (Rca) counteracts this issue by removing these inhibitors and thus maintaining Rubisco in its functional state. Inactivation o...

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Bibliographic Details
Main Author: Shivhare, Devendra
Other Authors: Oliver Martin Mueller-Cajar
Format: Thesis
Language:English
Published: 2017
Subjects:
Online Access:http://hdl.handle.net/10356/72402
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author Shivhare, Devendra
author2 Oliver Martin Mueller-Cajar
author_facet Oliver Martin Mueller-Cajar
Shivhare, Devendra
author_sort Shivhare, Devendra
collection NTU
description Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) forms inhibited complexes with its own substrate RuBP and other sugar phosphates. The AAA+ protein Rubisco activase (Rca) counteracts this issue by removing these inhibitors and thus maintaining Rubisco in its functional state. Inactivation of Rca at moderately high temperatures is associated with the loss of the activation state of Rubisco. Here we present a detailed characterization of the Rubisco activase from rice (Oryza sativa). We then compare its properties to a highly functional and thermostable Rca system from the desert plant, Agave tequilana. An extensive mutational study identified a number of residues that are likely involved in the Rubisco-Rca interaction. Finally we present a modified model for Rubisco activation in plants. Our results indicate that bioprospecting and careful biochemical characterization of Rca homologues will lead to both mechanistic insights and identification of candidate proteins for engineering enhanced thermotolerance in rice.
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spelling ntu-10356/724022023-02-28T18:46:52Z A molecular dissection of the Rubisco activation system from rice Shivhare, Devendra Oliver Martin Mueller-Cajar School of Biological Sciences DRNTU::Science::Biological sciences::Biochemistry Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) forms inhibited complexes with its own substrate RuBP and other sugar phosphates. The AAA+ protein Rubisco activase (Rca) counteracts this issue by removing these inhibitors and thus maintaining Rubisco in its functional state. Inactivation of Rca at moderately high temperatures is associated with the loss of the activation state of Rubisco. Here we present a detailed characterization of the Rubisco activase from rice (Oryza sativa). We then compare its properties to a highly functional and thermostable Rca system from the desert plant, Agave tequilana. An extensive mutational study identified a number of residues that are likely involved in the Rubisco-Rca interaction. Finally we present a modified model for Rubisco activation in plants. Our results indicate that bioprospecting and careful biochemical characterization of Rca homologues will lead to both mechanistic insights and identification of candidate proteins for engineering enhanced thermotolerance in rice. ​Doctor of Philosophy (SBS) 2017-07-10T01:34:55Z 2017-07-10T01:34:55Z 2017 Thesis Shivhare, D. (2017). A molecular dissection of the Rubisco activation system from rice. Doctoral thesis, Nanyang Technological University, Singapore. http://hdl.handle.net/10356/72402 10.32657/10356/72402 en 190 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences::Biochemistry
Shivhare, Devendra
A molecular dissection of the Rubisco activation system from rice
title A molecular dissection of the Rubisco activation system from rice
title_full A molecular dissection of the Rubisco activation system from rice
title_fullStr A molecular dissection of the Rubisco activation system from rice
title_full_unstemmed A molecular dissection of the Rubisco activation system from rice
title_short A molecular dissection of the Rubisco activation system from rice
title_sort molecular dissection of the rubisco activation system from rice
topic DRNTU::Science::Biological sciences::Biochemistry
url http://hdl.handle.net/10356/72402
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