Mass spectrometry reveals the assembly pathway of encapsulated ferritins and highlights a dynamic ferroxidase interface

Ross, Julia M.; Lambert, Thomas; Piergentili, Cecilia; He, Didi; Waldron, Kevin J.; Mackay, C. Logan; Marles‐Wright, Jon; Clarke, David J.

doi:10.1039/c9cc08130e

Cited by 19 publications

(6 citation statements)

References 20 publications

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“…[4] Ty pically,the gene encoding for Enc is located in atwo-gene operon with either ferritin (Flps) or hemerythrinslike proteins,o rd ye-decolorizing peroxidases (DyPs). [2,9] Selective packaging of co-expressed proteins is promoted by ac onserved amino-acid sequence (encapsulin localization sequence,E LS) at their C-terminus. [10][11][12] Importantly,n onnative cargo proteins can be directed inside Enc via simple tagging with ELS,e nabling self-assembly of the new functional compartment.…”

Section: Introductionmentioning

confidence: 99%

Inside a Shell—Organometallic Catalysis Inside Encapsulin Nanoreactors

et al. 2021

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Compartmentalization of chemical reactions inside cells are af undamental requirement for life.E ncapsulins are self-assembling protein-based nanocompartments from the prokaryotic repertoire that present ahighly attractive platform for intracellular compartmentalization of chemical reactions by design. Using single-molecule Fçrster resonance energy transfer and 3D-MINFLUX analysis,weanalyzefluorescently labeled encapsulins on as ingle-molecule basis.F urthermore, by equipping these capsules with asynthetic ruthenium catalyst via covalent attachment to an on-native host protein, we are able to perform in vitro catalysis and go on to showt hat engineered encapsulins can be used as hosts for transition metal catalysis inside living cells in confined space.

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Section: Introductionmentioning

confidence: 99%

Inside a Shell—Organometallic Catalysis Inside Encapsulin Nanoreactors

et al. 2021

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“…For instance, in the absence of cargo proteins, M. xanthus encapsulins form both T = 1 and T = 3 particles, but in the presence of the cargo, only T = 3 particles are formed [ 48 ]. On the other hand, Ross et al observed dimeric H. ochraceum FLPs in the absence of Fe +2 , suggesting that FLPs can also adopt different oligomeric states [ 56 ]. Interestingly, s-FLPs were initially classified as non-encapsulated FLPs since they lack a TP in their C-termini [ 57 ].…”

Section: Encapsulated Flpsmentioning

confidence: 99%

“…For example, ΔG is −7.8 kcal/M and −34.1 kcal/M for the A–A and B–B interfaces, respectively, of H. ochraceum EncFtn (Hoch_EncFtn, calculated by PISA, from the crystal structure PDB ID: 5n5f [ 28 ]). Ross et al performed an in-depth analysis of the Hoch_EncFtn pentamers of dimers assembly pathway using native mass spectrometry and hydrogen-deuterium exchange mass spectrometry [ 56 ]. Their analysis shows that decameric assembly formation is iron dependent and it is associated by the addition of the non–FOC dimers via the formation of the FOC interface upon iron binding.…”

Section: Encapsulated Flpsmentioning

confidence: 99%

Encapsulated Ferritin-like Proteins: A Structural Perspective

Eren,

Watts,

Montecinos

et al. 2024

Biomolecules

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Encapsulins are self–assembling nano–compartments that naturally occur in bacteria and archaea. These nano–compartments encapsulate cargo proteins that bind to the shell’s interior through specific recognition sequences and perform various metabolic processes. Encapsulation enables organisms to perform chemical reactions without exposing the rest of the cell to potentially harmful substances while shielding cargo molecules from degradation and other adverse effects of the surrounding environment. One particular type of cargo protein, the ferritin–like protein (FLP), is the focus of this review. Encapsulated FLPs are members of the ferritin–like protein superfamily, and they play a crucial role in converting ferrous iron (Fe+2) to ferric iron (Fe+3), which is then stored inside the encapsulin in mineralized form. As such, FLPs regulate iron homeostasis and protect organisms against oxidative stress. Recent studies have demonstrated that FLPs have tremendous potential as biosensors and bioreactors because of their ability to catalyze the oxidation of ferrous iron with high specificity and efficiency. Moreover, they have been investigated as potential targets for therapeutic intervention in cancer drug development and bacterial pathogenesis. Further research will likely lead to new insights and applications for these remarkable proteins in biomedicine and biotechnology.

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“…Applications of non-denaturing MS, often referred to native MS, are increasingly being used to investigate non-covalently bound protein cofactors, simple protein-protein complexes, or multi-protein super complexes [42,43]. Amongst studies of protein-cofactor interactions are an increasing number on proteins that contain metallo-cofactors [2,[44][45][46][47][48][49][50][51][52][53][54][55][56][57][58][59]. These have been particularly insightful where there is chemistry taking place at the cofactor, owing to the unique capability of native MS to simultaneously measure the accurate mass of multiple species, which may be different forms of the same protein, present in solution.…”

Section: Introductionmentioning

confidence: 99%