Jain, Gaurav, Pendola, Martin, Koutsoumpeli, Eleni orcid.org/0000-0002-3070-3319 et al. (2 more authors) (2018) Glycosylation Fosters Interactions between Model Sea Urchin Spicule Matrix Proteins. Implications for Embryonic Spiculogenesis and Biomineralization. Biochemistry. ISSN 1520-4995
Abstract
The formation of embryonic mineralized skeletal elements (spicules) in the sea urchin requires the participation of proteins, many of which may interact with one another and assist in the creation of an extracellular matrix wherein mineral formation takes place. To probe this, we created a sea urchin spicule recombinant model protein pair system wherein we tested the interactions between two major spicule proteins, SpSM50 and the glycoprotein, SpSM30B/C. Both proteins are strong hydrogelators that manipulate early and later events in mineral formation. We discovered that the anionic glycan moieties of SpSM30B/C are required for interaction with the SpSM50 protein and that these interactions are Ca(II)- independent. In addition, when these proteins form a complex, they create hybrid hydrogel particles that are physically distinct from their individual counterparts. Thus, glycan-mediated interactions play an important role in in vitro spicule protein assembly and most likely within the spicule itself.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018 American Chemical Society. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Electronic Engineering (York) |
Funding Information: | Funder Grant number EPSRC EP/P030017/1 |
Depositing User: | Pure (York) |
Date Deposited: | 25 May 2018 14:00 |
Last Modified: | 26 Jan 2025 00:12 |
Published Version: | https://doi.org/10.1021/acs.biochem.8b00207 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1021/acs.biochem.8b00207 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:131358 |