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

Journal Article · · Metallomics (Online)

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. Furthermore, 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.

Research Organization:
Brookhaven National Laboratory (BNL), Upton, NY (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division (CSGB); USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science (BSS); National Institutes of Health (NIH)
Grant/Contract Number:
SC0012704
OSTI ID:
2007526
Report Number(s):
BNL--224865-2023-JAAM
Journal Information:
Metallomics (Online), Journal Name: Metallomics (Online) Journal Issue: 11 Vol. 15; ISSN 1756-591X
Publisher:
Oxford University PressCopyright Statement
Country of Publication:
United States
Language:
English

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