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Nitropeptide Profiling and Identification Illustrated by Angiotensin II
Published on: June 16, 2019
Inhibition of AtMYB2 DNA-binding by nitric oxide involves cysteine S-nitrosylation
Viviane Serpa1, Javier Vernal, Lorenzo Lamattina
1Laboratório de Expressão Gênica, Departamento de Bioquímica, Universidade Federal de Santa Catarina, 88040-900 Florianópolis, SC, Brazil.
Abstract:
Nitric oxide (NO) can influence the transcriptional activity of a wide set of Arabidopsis genes. The aim of the present work was to investigate if NO modifies DNA-binding activity of AtMYB2 (a typical R2R3-MYB from Arabidopsis thaliana), by a posttranslational modification of its conserved Cys53 residue. We cloned a fully active minimal DNA-binding domain of AtMYB2 spanning residues 19-125, hereafter called M2D. In EMSA assays, M2D binds the core binding site 5'-[A]AACC[A]-3'. The NO donors SNP and GSNO inhibit M2D DNA-binding. As expected for a Cys S-nitrosylation, the NO-mediated inhibitory effect was reversed by DTT, and S-nitrosylation of Cys53 in M2D was detected by biotin switch assays. These results demonstrate that the DNA-binding of M2D is inhibited by S-nitrosylation of Cys53 as a consequence of NO action, thus establishing for the first time a relationship between the redox state and DNA-binding in a plant MYB transcription factor.
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