Inhibition of AtMYB2 DNA-binding by nitric oxide involves cysteine S-nitrosylation

Serpa, Viviane Isabel; Vernal, Javier; Lamattina, Lorenzo; Grotewold, Erich; Cassia, Raúl; Terenzi, Hernán

doi:10.1016/j.bbrc.2007.07.133

Cited by 116 publications

(59 citation statements)

References 26 publications

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“…The S-nitrosylation of Cys is probably the best characterized NO-mediated protein modification (for a review see Lindermayr & Durner 2009;Leitner et al 2009). In plants it was reported that NO regulates the binding of a MYB TF to DNA in vitro via S-nitrosylation (Serpa et al 2007).…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, it has been shown that: (1) the induction of CHS expression may be co-ordinately regulated by UV-B and nitric oxide (NO) (Mackerness et al 2001); and (2) NO regulates the binding of the AtMYB2 TF to DNA in vitro (Serpa et al 2007). NO is a ubiquitous bioactive molecule, produced in plants by enzymatic and nonenzymatic routes (see Wilson, Neill & (Beligni & Lamattina 2000).…”

Section: Introductionmentioning

confidence: 99%

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Retracted: Nitric oxide enhances plant ultraviolet‐B protection up‐regulating gene expression of the phenylpropanoid biosynthetic pathway

Tossi¹,

Amenta²,

Lamattina

et al. 2011

Plant Cell & Environment

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The link between ultraviolet (UV)-B, nitric oxide (NO) and phenylpropanoid biosynthetic pathway (PPBP) was studied in maize and Arabidopsis. The transcription factor (TF) ZmP regulates PPBP in maize. A genetic approach using P-rr (ZmP+) and P-ww (ZmP-) maize lines demonstrate that: (1) NO protects P-rr leaves but not P-ww from UV-B-induced reactive oxygen species (ROS) and cell damage; (2) NO increases flavonoid and anthocyanin content and prevents chlorophyll loss in P-rr but not in P-ww and (3)

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Retracted: Nitric oxide enhances plant ultraviolet‐B protection up‐regulating gene expression of the phenylpropanoid biosynthetic pathway

Tossi¹,

Amenta²,

Lamattina

et al. 2011

Plant Cell & Environment

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“…Thus, under non-reducing conditions, both cysteines form a disulfide bond that prevents the R2R3 MYB domain from binding to DNA (13,14). The DNA binding activity of another MYB family transcription factor, AtMYB2, which lacks the first Cys residue, is controlled by an alternative mechanism that involves cysteine S-nitrosylation (15). Thus, both oxidation and S-nitrosylation negatively influence the DNA binding activity of the MYB family transcription factors described (14,15).…”

mentioning

confidence: 99%

Redox-mediated Mechanisms Regulate DNA Binding Activity of the G-group of Basic Region Leucine Zipper (bZIP) Transcription Factors in Arabidopsis

Shaikhali

Norén

Barajas-López

et al. 2012

Journal of Biological Chemistry

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Background:The G-box cis-element is enriched in promoters of genes responding to light and to high light. Results: DTT induces DNA binding activity of bZIP transcription factors by reducing a disulfide bond. Conclusion: Redox regulation is crucial for DNA binding of the G-group of Arabidopsis bZIP transcription factors. Significance: Redox-dependent mechanisms modulate the activity of plant bZIPs in response to environmental signals.

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“…There are several examples of transcription factors whose activity is modified by redox agents in plants (Tron et al, 2002;Heine et al, 2004;Comelli and Gonzalez, 2007;Serpa et al, 2007;Shaikhali et al, 2008). The best studied case is perhaps the NPR1-TGA system (Després et al, 2003;Mou et al, 2003;Lindermayr et al, 2010).…”

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confidence: 99%

Redox Modulation of Plant Developmental Regulators from the Class I TCP Transcription Factor Family

2013

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TEOSINTE BRANCHED1-CYCLOIDEA-PROLIFERATING CELL FACTOR1 (TCP) transcription factors participate in plant developmental processes associated with cell proliferation and growth. Most members of class I, one of the two classes that compose the family, have a conserved cysteine at position 20 (Cys-20) of the TCP DNA-binding and dimerization domain. We show that Arabidopsis (Arabidopsis thaliana) class I proteins with Cys-20 are sensitive to redox conditions, since their DNAbinding activity is inhibited after incubation with the oxidants diamide, oxidized glutathione, or hydrogen peroxide or with nitric oxide-producing agents. Inhibition can be reversed by treatment with the reductants dithiothreitol or reduced glutathione or by incubation with the thioredoxin/thioredoxin reductase system. Mutation of Cys-20 in the class I protein TCP15 abolished its redox sensitivity. Under oxidizing conditions, covalently linked dimers were formed, suggesting that inactivation is associated with the formation of intermolecular disulfide bonds. Inhibition of class I TCP protein activity was also observed in vivo, in yeast (Saccharomyces cerevisiae) cells expressing TCP proteins and in plants after treatment with redox agents. This inhibition was correlated with modifications in the expression of the downstream CUC1 gene in plants. Modeling studies indicated that Cys-20 is located at the dimer interface near the DNA-binding surface. This places this residue in the correct orientation for intermolecular disulfide bond formation and explains the sensitivity of DNA binding to the oxidation of Cys-20. The redox properties of Cys-20 and the observed effects of cellular redox agents both in vitro and in vivo suggest that class I TCP protein action is under redox control in plants.TCP transcription factors constitute a family of plant developmental regulators (Martín-Trillo and Cubas, 2010;Uberti Manassero et al., 2013). The name of the family stands for the three first characterized members: TEOSINTE BRANCHED1, CYCLOIDEA, and PRO-LIFERATING CELL FACTOR1 (Cubas et al., 1999). These factors bind DNA through the TCP domain, a conserved region of approximately 60 amino acids that also participates in protein dimerization. The TCP domain contains a basic N-terminal region involved in DNA recognition, followed by a helix-loop-helix (HLH) motif similar to the one present in basic helix-loop-helix (bHLH) transcription factors (Aggarwal et al., 2010;Martín-Trillo and Cubas, 2010). Target sites recognized by TCP proteins are different from those bound by bHLH proteins (Kosugi and Ohashi, 2002;Viola et al., 2012). This is probably due to the fact that the respective basic regions differ markedly in composition and structure. Based on sequence homology, two main classes of TCP domains can be described. Class II proteins affect leaf and petal development and also influence shoot branching, among other processes

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Inhibition of AtMYB2 DNA-binding by nitric oxide involves cysteine S-nitrosylation

Cited by 116 publications

References 26 publications

Retracted: Nitric oxide enhances plant ultraviolet‐B protection up‐regulating gene expression of the phenylpropanoid biosynthetic pathway

Retracted: Nitric oxide enhances plant ultraviolet‐B protection up‐regulating gene expression of the phenylpropanoid biosynthetic pathway

Redox-mediated Mechanisms Regulate DNA Binding Activity of the G-group of Basic Region Leucine Zipper (bZIP) Transcription Factors in Arabidopsis

Redox Modulation of Plant Developmental Regulators from the Class I TCP Transcription Factor Family

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