Abstract
Thioredoxins are ubiquitous and conserved small proteins. The redox-active site is composed of highly conserved Cys32 and Cys35. In higher eukaryotes, thioredoxin evolved to a gain of function in nitrosative control, with 3 extra cysteines, Cys62, Cys69, and Cys73. Human thioredoxin 1 (hTrx) is directly involved in cellular signal transduction through S-nitrosation. The understanding of the mechanism of S-nitrosation is essential. Here we produced a mutant of hTrx containing only Cys62 (C62only). We report the almost full 1H, 15N, and 13C chemical shift assignment of the reduced and S-nitrosated C62only. This study will help to measure the reactivity Cys62 toward S-nitrosants and the stability of S-nitrosated Cys62.
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Acknowledgements
This work was funded by FAPERJ Grants 239229 and 204432, awarded to FCLA, CNPq Grant 309564/2017-4, awarded to FCLA. We thank INBEB-INCT for funding. The assignments were deposited at the Biomagnetic Resonance Data Bank (BMRB ID 50485 and 50484. We also thank the Rural Federal University of Rio de Janeiro (UFRRJ) for the release of V. S. Almeida to attend the doctorate at the Federal University of Rio de Janeiro (UFRJ).
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Almeida, V.S., Iqbal, A. & Almeida, F.C.L. 1H, 15N and 13C backbone and side‐chain assignments of reduced and S-nitrosated C62only mutant of human thioredoxin. Biomol NMR Assign 15, 261–265 (2021). https://doi.org/10.1007/s12104-021-10015-w
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DOI: https://doi.org/10.1007/s12104-021-10015-w