1H, 15N and 13C backbone and side‐chain assignments of reduced and S-nitrosated C62only mutant of human thioredoxin

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 dire...

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Published inBiomolecular NMR assignments Vol. 15; no. 2; pp. 261 - 265
Main Authors Almeida, Vitor S., Iqbal, Anwar, Almeida, Fabio C. L.
Format Journal Article
LanguageEnglish
Published Dordrecht Springer Netherlands 01.10.2021
Springer Nature B.V
Subjects
Biochemistry
Biological and Medical Physics
Biophysics
Mutants
Nitrosation
Physics
Physics and Astronomy
Polymer Sciences
Signal transduction
Thioredoxin
S-nitrosation
NMR
Thioredoxin
Post‐translational modification
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Summary: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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ISSN:1874-2718
1874-270X
1874-270X
DOI:10.1007/s12104-021-10015-w