Gu, Shuang, Bradley-Clarke, Jack, Rose, Ruth-Sarah, Warren, Martin J., Pickersgill, Richard W (2024) Enzyme-cargo encapsulation peptides bind between tessellating tiles of the bacterial microcompartment shell. The Journal of biological chemistry, . Article Number 107357. ISSN 0021-9258. E-ISSN 1083-351X. (doi:10.1016/j.jbc.2024.107357) (KAR id:106097)
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Official URL: https://doi.org/10.1016/j.jbc.2024.107357 |
Abstract
Bacterial microcompartments are prokaryotic organelles comprising encapsulated enzymes within a thin protein shell. They facilitate metabolic processing including propanediol, choline, glycerol, and ethanolamine utilization, and they accelerate carbon fixation in cyanobacteria. Enzymes targeted to the inside of the microcompartment frequently possess a cargo-encapsulation peptide, but the site to which the peptide binds is unclear. We provide evidence that the encapsulation peptides bind to the hydrophobic groove formed between tessellating subunits of the shell proteins. In silico docking studies provide a compelling model of peptide binding to this prominent hydrophobic groove. This result is consistent with the now widely accepted view that the convex side of the shell oligomers faces the lumen of the microcompartment. Binding of the encapsulation peptide to the groove between tessellating shell protein tiles explains why it has been difficult to define the peptide binding site using other methods, provides a mechanism by which encapsulation-peptide bearing enzymes can promote shell assembly, and explains how the presence of cargo affects the size and shape of the bacterial microcompartment. This knowledge may be exploited in engineering microcompartments or in disease prevention by hampering cargo-encapsulation.
Item Type: | Article |
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DOI/Identification number: | 10.1016/j.jbc.2024.107357 |
Additional information: | For the purpose of open access, the author has applied a CC BY public copyright licence to any Author Accepted Manuscript version arising from this submission. |
Uncontrolled keywords: | peptide interaction, bacterial metabolism, enzyme catalysis, protein self‐assembly, cell compartmentalization |
Subjects: |
Q Science Q Science > QH Natural history |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Funders: | Biotechnology and Biological Sciences Research Council (https://ror.org/00cwqg982) |
SWORD Depositor: | JISC Publications Router |
Depositing User: | JISC Publications Router |
Date Deposited: | 29 May 2024 14:41 UTC |
Last Modified: | 30 May 2024 01:27 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/106097 (The current URI for this page, for reference purposes) |
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