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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
bioRxiv : the preprint server for biology
2025
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| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41040395/ |
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Table of Contents:
- The CAGE complex: a hollow, megadalton, protein assembly in prokaryotic and eukaryotic microbes. McCafferty, Caitlyn L Hoogerbrugge, Gabriel Papoulas, Ophelia Schwartz, Evan A Ritchey, Simone Taylor, David W Brilot, Axel F Marcotte, Edward M We describe the identification and three-dimensional (3D) structure determination of an approx. 1 MDa, hollow, elliptical protein cage discovered while surveying proteins isolated from the ciliary matrix of the ciliate . By using mass spectrometry, AlphaFold, and cryo-electron microscopy, we identified the cage-like protein and determined its stoichiometry, mid-resolution 3D structure, and protein interactions. A sequence survey revealed several thousand homologs, with conservation across eukaryotic microbes spanning green algae, fungi, amoebozoans, choanoflagellates, and SAR organisms, as well as deep homology to genes in gram-negative predominantly marine prokaryotes and microbial mats, implying an ancient origin and arguing against a eukaryote-specific function. We subsequently isolated and solved the structure to high resolution from the slime mold . Based on these observations, we named this assembly the CAGE complex (for Conserved Assembly in Gram-negative bacteria and Eukaryotes). We speculate on potential roles as a chaperone, container, or protease trap, but the biological function of the CAGE complex has yet to be determined.