A virus capsid-like nanocompartment that stores iron and protects bacteria from oxidative stress
Colleen A. McHugh,Juan Fontana,Daniel Nemecek,Naiqian Cheng,Anastasia A. Aksyuk,J. Bernard Heymann,Dennis C. Winkler,Alan S Lam,Joseph S. Wall,Alasdair C. Steven,Egbert Hoiczyk +10 more
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TLDR
Physiological data reveal that few nanocompartments are assembled during vegetative growth, but they increase fivefold upon starvation, protecting cells from oxidative stress through iron sequestration.Abstract:
Living cells compartmentalize materials and enzymatic reactions to increase metabolic efficiency. While eukaryotes use membrane-bound organelles, bacteria and archaea rely primarily on protein-bound nanocompartments. Encapsulins constitute a class of nanocompartments widespread in bacteria and archaea whose functions have hitherto been unclear. Here, we characterize the encapsulin nanocompartment from Myxococcus xanthus, which consists of a shell protein (EncA, 32.5 kDa) and three internal proteins (EncB, 17 kDa; EncC, 13 kDa; EncD, 11 kDa). Using cryo-electron microscopy, we determined that EncA self-assembles into an icosahedral shell 32 nm in diameter (26 nm internal diameter), built from 180 subunits with the fold first observed in bacteriophage HK97 capsid. The internal proteins, of which EncB and EncC have ferritin-like domains, attach to its inner surface. Native nanocompartments have dense iron-rich cores. Functionally, they resemble ferritins, cage-like iron storage proteins, but with a massively greater capacity (~30,000 iron atoms versus ~3,000 in ferritin). Physiological data reveal that few nanocompartments are assembled during vegetative growth, but they increase fivefold upon starvation, protecting cells from oxidative stress through iron sequestration.read more
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Bacterial encapsulins as orthogonal compartments for mammalian cell engineering
Felix Sigmund,Christoph Massner,Philipp Erdmann,Anja Stelzl,Hannes Rolbieski,Mitul Desai,Sarah Bricault,Tobias P. Wörner,Joost Snijder,Arie Geerlof,Helmut Fuchs,Martin Hrabĕ de Angelis,Albert J. R. Heck,Alan Jasanoff,Vasilis Ntziachristos,Jürgen M. Plitzko,Gil G. Westmeyer +16 more
TL;DR: Eukaryotically expressed encapsulins enable cellular engineering of spatially confined multicomponent processes with versatile applications in multiscale molecular imaging, as well as intriguing implications for metabolic engineering and cellular therapy.
Journal ArticleDOI
Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments
Didi He,Sam Hughes,Sally Vanden-Hehir,Atanas Georgiev,Kirsten Altenbach,Emma Tarrant,C. Logan Mackay,Kevin J. Waldron,David Clarke,Jon Marles-Wright,Jon Marles-Wright +10 more
TL;DR: The structure and function is characterized of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid that has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface.
ComponentDOI
Large protein organelles form a new iron sequestration system with high storage capacity.
Tobias W. Giessen,Tobias W. Giessen,Tobias W. Giessen,Benjamin J. Orlando,Andrew A Verdegaal,Andrew A Verdegaal,Melissa G. Chambers,Jules Gardener,David C. Bell,Gabriel Birrane,Maofu Liao,Maofu Liao,Pamela A. Silver +12 more
TL;DR: In this article, structural and mechanistic characterization of a 42 nm two-component encapsulin-based iron storage compartment from Quasibacillus thermotolerans is reported.
Journal ArticleDOI
Encapsulins: molecular biology of the shell
TL;DR: The current understanding of encapsulin structure and function is reviewed and exciting open questions of physiological significance are highlighted, suggesting that nanocompartments play an important role in many microbes.
Journal ArticleDOI
Structural Characterization of Native and Modified Encapsulins as Nanoplatforms for in Vitro Catalysis and Cellular Uptake
Rindia M. Putri,Carolina Allende-Ballestero,Daniel Luque,Daniel Luque,Robin Klem,Katerina Asteria Rousou,Aijie Liu,Christoph H.-H. Traulsen,W Frederik Rurup,Melissa S. T. Koay,José R. Castón,Jeroen J. L. M. Cornelissen +11 more
TL;DR: The native structure of B. linens encapsulins with both native and foreign cargo is characterized using cryo-electron microscopy and the functionality of the encapsulin for an in vitro surface-immobilized catalysis in a cascade pathway with an additional enzyme, glucose oxidase is demonstrated.
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