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In vitro maturation of NiSOD reveals a role for cytoplasmic histidine in processing and metalation.
- Source :
-
Metallomics : integrated biometal science [Metallomics] 2023 Nov 02; Vol. 15 (11). - Publication Year :
- 2023
-
Abstract
- The importance of cellular low molecular weight 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.<br /> (© The Author(s) 2023. Published by Oxford University Press.)
Details
- Language :
- English
- ISSN :
- 1756-591X
- Volume :
- 15
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Metallomics : integrated biometal science
- Publication Type :
- Academic Journal
- Accession number :
- 37723610
- Full Text :
- https://doi.org/10.1093/mtomcs/mfad054