Balanced Regulation of Redox Status of Intracellular Thioredoxin Revealed by in-Cell NMR.
J Am Chem Soc. 2018 Mar 06;:
Authors: Mochizuki A, Saso A, Zhao Q, Kubo S, Nishida N, Shimada I
Abstract
To understand how intracellular proteins respond to oxidative stresses, the redox status of the target protein, as well as the intracellular redox potential ( EGSH), which is defined by the concentrations of reduced and oxidized glutathione, should be observed simultaneously within living cells. In this study, we developed a method that can monitor the redox status of thioredoxin (Trx) and EGSH by direct NMR observation of Trx and glutathione within living cells. Unlike the midpoint potential of Trx measured in vitro (~ -300 mV), the intracellular Trx exhibited the redox transition at EGSH between -250 and -200 mV, the range known to trigger the oxidative stress-mediated signalings. Furthermore, we quantified the contribution of Trx reductase to the redox status of Trx, demonstrating that the redox profile of Trx is determined by the interplay between the elevation of EGSH and the reduction by Trx reductase and other endogenous molecules.
PMID: 29509009 [PubMed - as supplied by publisher]
BalancedRegulation of Redox Status of IntracellularThioredoxin Revealed by in-Cell NMR
BalancedRegulation of Redox Status of IntracellularThioredoxin Revealed by in-Cell NMR
Ayano Mochizuki, Arata Saso, Qingci Zhao, Satoshi Kubo, Noritaka Nishida and Ichio Shimada
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b00426/20180306/images/medium/ja-2018-004263_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b00426
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Direct structural evidence of protein redox regulation obtained by in-cell NMR
Direct structural evidence of protein redox regulation obtained by in-cell NMR
Publication date: Available online 14 November 2015
Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research</br>
Author(s): Eleonora Mercatelli, Letizia Barbieri, Enrico Luchinat, Lucia Banci</br>
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