Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is responsible for almost all biological CO2 assimilation, but forms inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. The distantly related AAA+ proteins rubisco activase and CbbX remodel inh...
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sg-ntu-dr.10356-838872023-02-28T17:03:40Z Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria Tsai, Yi-Chin Candace Lapina, Maria Claribel Bhushan, Shashi Mueller-Cajar, Oliver School of Biological Sciences Enzyme Mechanisms Bacteriology Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is responsible for almost all biological CO2 assimilation, but forms inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. The distantly related AAA+ proteins rubisco activase and CbbX remodel inhibited rubisco complexes to effect inhibitor release in plants and α-proteobacteria, respectively. Here we characterize a third class of rubisco activase in the chemolithoautotroph Acidithiobacillus ferrooxidans. Two sets of isoforms of CbbQ and CbbO form hetero-oligomers that function as specific activases for two structurally diverse rubisco forms. Mutational analysis supports a model wherein the AAA+ protein CbbQ functions as motor and CbbO is a substrate adaptor that binds rubisco via a von Willebrand factor A domain. Understanding the mechanisms employed by nature to overcome rubisco’s shortcomings will increase our toolbox for engineering photosynthetic carbon dioxide fixation. MOE (Min. of Education, S’pore) Published version 2017-07-14T05:16:59Z 2019-12-06T15:33:55Z 2017-07-14T05:16:59Z 2019-12-06T15:33:55Z 2015 Journal Article Tsai, Y.-C. C., Lapina, M. C., Bhushan, S., & Mueller-Cajar, O. (2015). Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria. Nature Communications, 6, 8883-. 2041-1723 https://hdl.handle.net/10356/83887 http://hdl.handle.net/10220/42865 10.1038/ncomms9883 26567524 en Nature Communications © 2015 The Author(s). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ 10 p. application/pdf |
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Enzyme Mechanisms Bacteriology Tsai, Yi-Chin Candace Lapina, Maria Claribel Bhushan, Shashi Mueller-Cajar, Oliver Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria |
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Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is responsible for almost all biological CO2 assimilation, but forms inhibited complexes with its substrate ribulose-1,5-bisphosphate (RuBP) and other sugar phosphates. The distantly related AAA+ proteins rubisco activase and CbbX remodel inhibited rubisco complexes to effect inhibitor release in plants and α-proteobacteria, respectively. Here we characterize a third class of rubisco activase in the chemolithoautotroph Acidithiobacillus ferrooxidans. Two sets of isoforms of CbbQ and CbbO form hetero-oligomers that function as specific activases for two structurally diverse rubisco forms. Mutational analysis supports a model wherein the AAA+ protein CbbQ functions as motor and CbbO is a substrate adaptor that binds rubisco via a von Willebrand factor A domain. Understanding the mechanisms employed by nature to overcome rubisco’s shortcomings will increase our toolbox for engineering photosynthetic carbon dioxide fixation. |
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School of Biological Sciences |
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School of Biological Sciences Tsai, Yi-Chin Candace Lapina, Maria Claribel Bhushan, Shashi Mueller-Cajar, Oliver |
format |
Article |
author |
Tsai, Yi-Chin Candace Lapina, Maria Claribel Bhushan, Shashi Mueller-Cajar, Oliver |
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Tsai, Yi-Chin Candace |
title |
Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria |
title_short |
Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria |
title_full |
Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria |
title_fullStr |
Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria |
title_full_unstemmed |
Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria |
title_sort |
identification and characterization of multiple rubisco activases in chemoautotrophic bacteria |
publishDate |
2017 |
url |
https://hdl.handle.net/10356/83887 http://hdl.handle.net/10220/42865 |
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1759857122311405568 |