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In vitro maturation of NiSOD reveals a role for cytoplasmic histidine in processing and metalation

Basak, Priyanka; Cabelli, Diane E.; Chivers, Peter T.; Farquhar, Erik R.; Maroney, Michael J.

Authors

Priyanka Basak

Diane E. Cabelli

Erik R. Farquhar

Michael J. Maroney



Abstract

The importance of cellular low molecular weight (LMW) ligands in metalloenzyme maturation is largely unexplored. Maturation of NiSOD requires post-translational N-terminal processing of the proenzyme, SodN, by its cognate protease, SodX. Here we provide evidence for the participation of L-histidine in the protease-dependent maturation of Nickel-dependent Superoxide Dismutase (NiSOD) from Streptomyces coelicolor. In vitro studies using purified proteins cloned from S. coelicolor and overexpressed in E. coli support a model where a ternary complex formed between the substrate (SodN), the protease (SodX) and L-Histidine creates a novel Ni-binding site that is capable of the N-terminal processing of SodN and specifically incorporates Ni into the apo-NiSOD product. Thus, L-Histidine serves many of the functions associated with a metallochaperone or, conversely, eliminates the need for a metallochaperone in NiSOD maturation.

Citation

Basak, P., Cabelli, D. E., Chivers, P. T., Farquhar, E. R., & Maroney, M. J. (2023). In vitro maturation of NiSOD reveals a role for cytoplasmic histidine in processing and metalation. Metallomics, 15(11), Article mfad054. https://doi.org/10.1093/mtomcs/mfad054

Journal Article Type Article
Acceptance Date Sep 16, 2023
Online Publication Date Sep 18, 2023
Publication Date 2023-11
Deposit Date Sep 19, 2023
Publicly Available Date Sep 19, 2024
Journal Metallomics
Print ISSN 1756-5901
Publisher Oxford University Press
Peer Reviewed Peer Reviewed
Volume 15
Issue 11
Article Number mfad054
DOI https://doi.org/10.1093/mtomcs/mfad054
Public URL https://durham-repository.worktribe.com/output/1742242