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ATP induces folding of ALS-causing C71G-hPFN1 and nascent hSOD1

Biology

ATP induces folding of ALS-causing C71G-hPFN1 and nascent hSOD1

J. Kang, L. Lim, et al.

Discover how ATP transforms C71G-hPFN1 into a fully folded state and induces nascent hSOD1 into a mix of folded and unfolded states. This exciting research by Jian Kang, Liangzhong Lim, and Jianxing Song sheds light on the potential role of polyphosphates as primordial chaperones and offers valuable insights into age-related familial ALS onset.

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Playback language: English
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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