Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/83887
Title: Identification and characterization of multiple rubisco activases in chemoautotrophic bacteria
Authors: Tsai, Yi-Chin Candace
Lapina, Maria Claribel
Bhushan, Shashi
Mueller-Cajar, Oliver
Keywords: Enzyme Mechanisms
Bacteriology
Issue Date: 2015
Source: 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-.
Series/Report no.: Nature Communications
Abstract: 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.
URI: https://hdl.handle.net/10356/83887
http://hdl.handle.net/10220/42865
ISSN: 2041-1723
DOI: 10.1038/ncomms9883
Rights: © 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/
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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