From Transcription Factors to Designed Sequence‐Specific DNA‐Binding Peptides

Vázquez, M. Eugenio; Caamaño, Ana M.; Mascareñas, José L.

doi:10.1002/chin.200406287

Cited by 11 publications

(15 citation statements)

References 1 publication

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“…Multimerization of transcription factors is often essential for DNA binding (Vázquez et al ., ; Marianayagam et al ., ). We therefore hypothesized that phosphorylation might disrupt AKS1 multimers, thereby inhibiting the binding of AKS1 to DNA.…”

Section: Resultsmentioning

confidence: 99%

Inhibition of the Arabidopsis bHLH transcription factor by monomerization through abscisic acid‐induced phosphorylation

et al. 2016

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SUMMARYWe have demonstrated that the Arabidopsis basic helix-loop-helix (bHLH) transcription factor, ABA-responsive kinase substrate 1 (AKS1; also known as FLOWERING BHLH 3, FBH3), enhances K + channel expression in guard cells leading to stomatal opening. The expression is suppressed by ABA-induced phosphorylation of AKS1. Here we show that the phosphorylation results in the monomerization of AKS1 multimers and inhibits AKS1 binding to DNA. AKS1 forms homo-multimers which dissociate following phosphorylation. Replacement of a critical amino acid in the bHLH domain inhibited multimer formation and decreased the binding of AKS1 to DNA. The monomerization was elicited via phosphorylation at three serine residues, which is mediated by SNF1-related protein kinase 2.6 (SnRK2.6), in the vicinity of bHLH domain. Furthermore, ABA induced the phosphorylation-dependent release of AKS1 from DNA, thereby suppressing transcriptional activity in vivo. Our results document a mechanism that inhibits gene expression by phosphorylation of a bHLH transcription factor.

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Section: Resultsmentioning

confidence: 99%

Inhibition of the Arabidopsis bHLH transcription factor by monomerization through abscisic acid‐induced phosphorylation

et al. 2016

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“…sugar-phosphate backbone binding; intercalation between the base pairs and covalent binding or metal-coordination to the bases. Meanwhile major groove recognition is mainly preferred by proteins and DNA which will be describe below (46), minor groove recognition and intercalation is preferred by synthetic agents (47). Incorporation of a transition metal into an intercalator is an attractive way of imparting positive charge to the complex.…”

Section: Dna Structure and Stabilitymentioning

confidence: 99%

Biomolecular studies by circular dichroism

Dodero

Quirolo²,

Sequeira³

2011

Front Biosci

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“…In the present work, we use ESI mass spectrometry to investigate the gas‐phase stability and dissociation pathways of non‐covalent DNA–peptide complexes. Different types of interactions are able to stabilise DNA complexes in solution,16 including hydrogen bonds, van der Waals, hydrophobic and electrostatic interactions. There is no consensus on the quantitative contribution of these interactions.…”

Section: Introductionmentioning

confidence: 99%

Charge state effect on the zwitterion influence on stability of non‐covalent interaction of single‐stranded DNA with peptides

2007

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Negative ion ESI mass spectrometry was used to study the gas-phase stability and dissociation pathways of peptide-DNA complexes. We show that bradykinin and three modified peptides containing the basic residue arginine or lysine form stable interactions with single-stranded oligonucleotides. ESI-MS/MS of complexes of T(8) with PPGFSPFRR resulted in a major dissociation pathway through cleavage of the peptide covalent bond. The stability of the complex is due to electrostatic interaction between the negatively charged phosphate group and the basic side chain of the arginine and lysine residues as demonstrated by Vertes et al. and Woods et al. In fact, the present work establishes the role played by zwitterions on complex stabilisation. The presence of protons in nucleobase and/or amino acid contributes in reinforcing the strength of the salt bridge (SB) interaction. The zwitterionic form of the most basic of amino acid residues, arginine, is assumed to form a strong SB interaction to the negatively charged phosphate groups of DNA. This non-covalent complex is stable enough to withstand disruption of the non-covalent interaction and to first break the covalent bond. Moreover, the dependence of fragmentation patterns upon the complex charge state is explained by the fact that the net number of negative charges modulates the number of zwitterionic sites, which stabilise the complexes. Finally, the weak influence of the nucleobase is assumed by the existence of competition for proton addition between the nucleobase and the R/K side chain leading to a decrease in the stabilisation of the SB interaction.

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From Transcription Factors to Designed Sequence‐Specific DNA‐Binding Peptides

Abstract: For Abstract see ChemInform Abstract in Full Text.

Cited by 11 publications

References 1 publication

Inhibition of the Arabidopsis bHLH transcription factor by monomerization through abscisic acid‐induced phosphorylation

Inhibition of the Arabidopsis bHLH transcription factor by monomerization through abscisic acid‐induced phosphorylation

Biomolecular studies by circular dichroism

Charge state effect on the zwitterion influence on stability of non‐covalent interaction of single‐stranded DNA with peptides

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