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Abstract
ALS-causing C71G-hPFN1 exists in folded and unfolded states, while nascent hSOD1 is unfolded. This study uses NMR to show that ATP converts C71G-hPFN1 completely into its folded state (1:2 ratio), and induces nascent hSOD1 into a mixture of folded and unfolded states (1:8 ratio). ATP's triphosphate group is responsible for this effect, but free triphosphate causes aggregation. The mechanism involves ATP enhancing the intrinsic folding capacity of the proteins. The findings suggest a role for polyphosphates as primordial chaperones and offer insight into age-related familial ALS onset.
Publisher
Communications Chemistry
Published On
Jun 15, 2023
Authors
Jian Kang, Liangzhong Lim, Jianxing Song
Tags
ALS
ATP
C71G-hPFN1
hSOD1
polyphosphates
protein folding
NMR
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