The material properties of cellulose are heavily influenced by the organisation of β-1,4-glucan chains into a microfibril. It is likely that the structure of this microfibril is determined by the spatial arrangement of catalytic cellulose synthase (CESA) proteins within the cellulose synthase complex (CSC). In land plants, CESA proteins form a large complex composed of a hexamer of trimeric lobes termed the rosette. Each rosette synthesises a single microfibril likely composed of 18 glucan chains. In this review, the biochemical events leading to plant CESA protein assembly into the rosette are explored. The protein interfaces responsible for CESA trimerization are formed by regions that define rosette-forming CESA proteins. As a consequence, these regions are absent from the ancestral bacterial cellulose synthases (BcsAs) that do not form rosettes. CSC assembly occurs within the context of the endomembrane system, however the site of CESA assembly into trimers and rosettes is not determined. Both the N-Terminal Domain and Class Specific Region of CESA proteins are intrinsically disordered and contain all of the identified phosphorylation sites, making both regions candidates as sites for protein–protein interactions and inter–lobe interface formation. We propose a sequential assembly model, whereby CESA proteins form stable trimers shortly after native folding, followed by sequential recruitment of lobes into a rosette, possibly assisted by Golgi-localised STELLO proteins. A comprehensive understanding of CESA assembly into the CSC will enable directed engineering of CESA protein spatial arrangements, allowing changes in cellulose crystal packing that alter its material properties.
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February 2021
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On the implications of the copper co-factor in lytic polysaccharide monooxygenase. A brief overview of structure, oxygen activation and application as bioindustrial process tools for decomposition of lignocellulose. Further information can be found in the review by Ipsen and colleagues (pages 531–540). Image provided by Katja Johansen.
Review Article|
February 22 2021
The molecular basis of plant cellulose synthase complex organisation and assembly
Thomas H Wilson;
Thomas H Wilson
Faculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, U.K.
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Manoj Kumar;
Manoj Kumar
Faculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, U.K.
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Simon R Turner
Faculty of Biology, Medicine and Health, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, U.K.
Correspondence: Simon R Turner (simon.turner@manchester.ac.uk)
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Biochem Soc Trans (2021) 49 (1): 379–391.
Article history
Received:
November 11 2020
Revision Received:
January 25 2021
Accepted:
January 29 2021
Citation
Thomas H Wilson, Manoj Kumar, Simon R Turner; The molecular basis of plant cellulose synthase complex organisation and assembly. Biochem Soc Trans 26 February 2021; 49 (1): 379–391. doi: https://doi.org/10.1042/BST20200697
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