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PreprintCited by 25Enzyme function and inhibitionPhotosynthetic Processes and MechanismsMetalloenzymes and iron-sulfur proteins

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Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP

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Pulsford, Sacha B., Outram, Megan A., Förster, Britta, Rhodes, Timothy, Williams, Simon J., Badger, Murray R., Price, G. Dean, Jackson, Colin J., Long, Benedict M.·2023·Science Advances
DOI 10.1101/2023.07.31.551272PMC PMC11086599

Preprint — published as 10.1126/sciadv.adk7283 · Paper page

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Abstract

Cyanobacterial CO 2 concentrating mechanisms (CCMs) sequester a globally significant proportion of carbon into the biosphere. Proteinaceous microcompartments, called carboxysomes, play a critical role in CCM function, housing two enzymes to enhance CO 2 fixation: carbonic anhydrase (CA) and Rubisco. Despite its importance, our current understanding of the carboxysomal CAs found in ɑ-cyanobacteria, CsoSCA, remains limited, particularly regarding the regulation of its activity. Here, we present the first structural and biochemical study of CsoSCA from the cyanobacterium Cyanobium PCC7001 . Our results show that the Cyanobium CsoSCA is allosterically activated by the Rubisco substrate ribulose-1,5-bisphosphate (RuBP), and forms a hexameric trimer of dimers. Comprehensive phylogenetic and mutational analyses are consistent with this regulation appearing exclusively in cyanobacterial ɑ-carboxysome CAs. These findings clarify the biologically relevant oligomeric state of α-carboxysomal CAs and advance our understanding of the regulation of photosynthesis in this globally dominant lineage. One-Sentence Summary: The carboxysomal carbonic anhydrase, CsoSCA, is allosterically activated by the Rubisco substrate RuBP, revealing a novel mechanism controlling key enzyme activity in cyanobacterial α-carboxysomes.

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Metadata

Authors
Pulsford, S. B., Outram, M. A., Förster, B., Rhodes, T., Williams, S. J., Badger, M. R., Price, G. D., Jackson, C. J., & Long, B. M.
Affiliations
  • Australian National University (AU)
  • ARC Centre of Excellence in Synthetic Biology (AU)
Corresponding author
Long, Benedict M.
ORCID
Venue
Science Advances
Publisher
openRxiv
Published
2023-07-31
Volume
10
Issue
19
Pages
eadk7283-eadk7283
ISSN
2375-2548 (ISSN-L)
DOI
10.1101/2023.07.31.551272
PMC
PMC11086599
OpenAlex
W4396815382
Cited by
25
References
1
Citations by year
2026: 13 · 2025: 6 · 2024: 4 · 2023: 2
FWCI
3.13
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Science Advances (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • ANU Open Research (Australian National University) (submittedVersion)
  • NOVA (University of Newcastle Australia) (submittedVersion)
Funders
  • Australian Nuclear Science and Technology Organisation
  • Australian Cancer Research Foundation
  • Australian Synchrotron
  • Westpac Scholars Trust
  • Australian Research Council (CE140100015, CE200100029)
  • ARC Centre of Excellence for Translational Photosynthesis (CE140100015)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme function and inhibition
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
Keywords
carboxysomes, carbonic anhydrase, allosteric regulation, ribulose-1,5-bisphosphate, CO2-concentrating mechanism, oligomeric state, protein structure, photosynthesis regulation, cyanobacteria
MeSH terms
Cyanobacteria, Allosteric Regulation, Bacterial Proteins, Carbon Dioxide, Carbonic Anhydrases, Models, Molecular, Phylogeny, Ribulose-Bisphosphate Carboxylase, Ribulosephosphates, Substrate Specificity, Protein Multimerization

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