Human glutaredoxin-1 can transfer copper to isolated metal binding domains of the P1B-type ATPase, ATP7B.

Scientific Reports
Shadi MaghoolMegan J Maher

Abstract

Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human enzyme glutaredoxin-1 (hGrx1) has been shown to possess Cu metallochaperone activity. The aim of this study was to ascertain whether hGrx1 can act in Cu delivery to the metal binding domains (MBDs) of the P1B-type ATPase ATP7B and to determine the thermodynamic factors that underpin this activity. hGrx1 can transfer Cu to the metallochaperone Atox1 and to the MBDs 5-6 of ATP7B (WLN5-6). This exchange is irreversible. In a mixture of the three proteins, Cu is delivered to the WLN5-6 preferentially, despite the presence of Atox1. This preferential Cu exchange appears to be driven by both the thermodynamics of the interactions between the proteins pairs and of the proteins with Cu(I). Crucially, protein-protein interactions between hGrx1, Atox1 and WLN5-6 were detected by NMR spectroscopy both in the presence and absence of Cu at a common interface. This study augments the possible activities of hGrx1 in intracellular Cu homeostasis and suggests a potential redundancy in this system, whe...Continue Reading

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Citations

Jun 9, 2020·Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine·Xiaolu ZhangPernilla Wittung-Stafshede
Oct 23, 2020·Biochimica Et Biophysica Acta. Molecular Cell Research·Vinit C ShanbhagMichael J Petris
Oct 1, 2021·Frontiers in Microbiology·Andreea AndreiHans-Georg Koch

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Methods Mentioned

BETA
NMR
two-hybrid
co-immunoprecipitation
size exclusion chromatography
nuclear magnetic resonance
electron exchange
PCR
size-exclusion chromatography

Software Mentioned

PyMOL
SPARKY
PyMOL Molecular Graphics System
Origin2016

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