Thioredoxins are a family of conserved oxidoreductases responsible for maintaining redox balance within cells. They have also served as excellent model systems for protein design and engineering studies particularly through ancestral sequence reconstruction methods. The recent work by Gamiz-Arco et al. [Biochem J (2019) 476, 3631–3647] answers fundamental questions on how specific sequence differences can contribute to differences in folding rates between modern and ancient thioredoxins but also among a selected subset of modern thioredoxins. They surprisingly find that rapid unassisted folding, a feature of ancient thioredoxins, is not conserved in the modern descendants suggestive of co-evolution of better folding machinery that likely enabled the accumulation of mutations that slow-down folding. The work thus provides an interesting take on the expected folding-stability-function constraint while arguing for additional factors that contribute to sequence evolution and hence impact folding efficiency.
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March 2020
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The sensor protein H-NOX from Vibrio cholerae can be reversibly activated by oxidation of cysteine residues to a zinc binding site. Computational models along with EXAFS and mass spectrometry data reveal the details of this process. For further information, see the article by Mukhopadhyay and colleagues (pp. 1123–1136) in this issue. The image was provided by Erik Yukl.
Commentary|
March 18 2020
Molecular origins of folding rate differences in the thioredoxin family
Athi N. Naganathan
Department of Biotechnology, Bhupat & Jyoti Mehta School of Biosciences, Indian Institute of Technology Madras, Chennai 600036, India
Correspondence: Athi N. Naganathan ([email protected])
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Publisher: Portland Press Ltd
Received:
December 26 2019
Revision Received:
February 19 2020
Accepted:
February 20 2020
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2020 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2020
Biochem J (2020) 477 (6): 1083–1087.
Article history
Received:
December 26 2019
Revision Received:
February 19 2020
Accepted:
February 20 2020
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Citation
Athi N. Naganathan; Molecular origins of folding rate differences in the thioredoxin family. Biochem J 27 March 2020; 477 (6): 1083–1087. doi: https://doi.org/10.1042/BCJ20190864
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