A metal-trap tests and refines blueprints to engineer cellular protein metalation with different elements

Sophie E. Clough, Tessa R. Young, Emma Tarrant, Andrew J. P. Scott, Peter T. Chivers, Arthur Glasfeld and Nigel J. Robinson ()
Additional contact information
Sophie E. Clough: University of Durham
Tessa R. Young: University of Durham
Emma Tarrant: University of Durham
Andrew J. P. Scott: University of Durham
Peter T. Chivers: University of Durham
Arthur Glasfeld: University of Durham
Nigel J. Robinson: University of Durham

Nature Communications, 2025, vol. 16, issue 1, 1-15

Abstract: Abstract It has been challenging to test how proteins acquire specific metals in cells. The speciation of metalation is thought to depend on the preferences of proteins for different metals competing at intracellular metal-availabilities. This implies mis-metalation may occur if proteins become mis-matched to metal-availabilities in heterologous cells. Here we use a cyanobacterial MnII-cupin (MncA) as a metal trap, to test predictions of metalation. By re-folding MncA in buffered competing metals, metal-preferences are determined. Relating metal-preferences to metal-availabilities estimated using cellular metal sensors, predicts mis-metalation of MncA with FeII in E. coli. After expression in E. coli, predominantly FeII-bound MncA is isolated experimentally. It is predicted that in metal-supplemented viable cells metal-MncA speciation should switch. MnII-, CoII-, or NiII-MncA are recovered from the respective metal-supplemented cells. Differences between observed and predicted metal-MncA speciation are used to refine estimated metal availabilities. Values are provided as blueprints to guide engineering biological protein metalation.

Date: 2025
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-025-56199-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-56199-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-025-56199-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().