Mackinder, Luke orcid.org/0000-0003-1440-3233, Chen, Chris, Leib, Ryan et al. (6 more authors) (2017) A spatial interactome reveals the protein organization of the algal CO2 concentrating mechanism. Cell. e14. pp. 133-147. ISSN 1097-4172
Abstract
Approximately one-third of global CO 2 fixation is performed by eukaryotic algae. Nearly all algae enhance their carbon assimilation by operating a CO 2-concentrating mechanism (CCM) built around an organelle called the pyrenoid, whose protein composition is largely unknown. Here, we developed tools in the model alga Chlamydomonas reinhardtii to determine the localizations of 135 candidate CCM proteins and physical interactors of 38 of these proteins. Our data reveal the identity of 89 pyrenoid proteins, including Rubisco-interacting proteins, photosystem I assembly factor candidates, and inorganic carbon flux components. We identify three previously undescribed protein layers of the pyrenoid: a plate-like layer, a mesh layer, and a punctate layer. We find that the carbonic anhydrase CAH6 is in the flagella, not in the stroma that surrounds the pyrenoid as in current models. These results provide an overview of proteins operating in the eukaryotic algal CCM, a key process that drives global carbon fixation.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | © 2017 Elsevier Inc. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. |
Keywords: | CCM,CO -concentrating mechanism,Chlamydomonas reinhardtii,Rubisco,affinity purification mass spectrometry,carbon fixation,high-throughput fluorescence protein tagging,photosynthesis,pyrenoid |
Dates: |
|
Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) |
Depositing User: | Pure (York) |
Date Deposited: | 30 Aug 2017 08:00 |
Last Modified: | 08 Feb 2025 00:24 |
Published Version: | https://doi.org/10.1016/j.cell.2017.08.044 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1016/j.cell.2017.08.044 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:120655 |
Downloads
Filename: CELL_D_17_00826R2_Manuscript.pdf
Description: CELL-D-17-00826R2_Manuscript
Filename: Mackinder_CELL_D_17_00826R1_Manuscript.pdf
Description: Mackinder - CELL-D-17-00826R1_Manuscript