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

Lookup NU author(s): Dr Cecilia Piergentili, Dr Kevin WaldronORCiD, Dr Jon Marles-WrightORCiD

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This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0).

Abstract

This journal is © The Royal Society of Chemistry.Encapsulated ferritins (EncFtn) are a recently characterised member of the ferritin superfamily. EncFtn proteins are sequestered within encapsulin nanocompartments and form a unique biological iron storage system. Here, we use native mass spectrometry and hydrogen-deuterium exchange mass spectrometry to elucidate the metal-mediated assembly pathway of EncFtn.

Publication metadata

Author(s): Ross J, Lambert T, Piergentili C, He D, Waldron KJ, Mackay CL, Marles-Wright J, Clarke DJ

Publication type: Article

Publication status: Published

Journal: Chemical Communications

Year: 2020

Volume: 56

Issue: 23

Pages: 3417-3420

Online publication date: 13/02/2020

Acceptance date: 13/02/2020

Date deposited: 06/04/2020

ISSN (print): 1359-7345

ISSN (electronic): 1364-548X

Publisher: Royal Society of Chemistry

URL: https://doi.org/10.1039/C9CC08130E

DOI: 10.1039/c9cc08130e

PubMed id: 32090213

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Funding

Funder referenceFunder name
BB/N005570/1Biotechnology and Biological Sciences Research Council (BBSRC)
BB/M010996/1
BB/R013993/1
EPSRC

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