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.

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
• Electronic ISSN: 1756-591X
• 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