An Amyloid Organelle: Solid State NMR Evidence for Cross-Beta Assembly of Gas Vesicles
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gv_amyloid_jbc_05.pdf
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Author(s)
Bayro, Marvin J.
Daviso, Eugenio
Belenky, Marina
Griffin, Robert Guy
Herzfeld, Judith
Date Issued
January 2012
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry and Molecular Biology
Citation
Bayro, M. J. et al. “An Amyloid Organelle, Solid-state NMR Evidence for Cross- Assembly of Gas Vesicles.” Journal of Biological Chemistry 287.5 (2011): 3479–3484. Web.
Version
Author's final manuscript
Abstract
Functional amyloids have been identified in a wide range of organisms, taking on a variety of biological roles and being controlled by remarkable mechanisms of directed assembly. Here, we report that amyloid fibrils constitute the ribs of the buoyancy organelles of Anabaena flos-aquae. The walls of these gas-filled vesicles are known to comprise a single protein, GvpA, arranged in a low pitch helix. However, the tertiary and quaternary structures have been elusive. Using solid-state NMR correlation spectroscopy we find detailed evidence for an extended cross-β structure. This amyloid assembly helps to account for the strength and amphiphilic properties of the vesicle wall. Buoyancy organelles thus dramatically extend the scope of known functional amyloids.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology)
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Creative Commons Attribution-Noncommercial-Share Alike 3.0
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DOI of Published Version
https://doi.org/10.1074/jbc.M111.313049
