FEBS Letters
Volume 580, Issue 8 , Pages 1919-1924, 3 April 2006

Specificity in DNA recognition by a peptide from papillomavirus E2 protein

Edited by Ivan Sadowski

  • Joana Faber-Barata

      Affiliations

    • Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, CCS, sala Bs-34, Ilha do Fundão, 21941-590, Rio de Janeiro, RJ, Brazil
    • Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Ilha do Fundão, 21941-590, Rio de Janeiro, RJ, Brazil
    • ,
  • Ronaldo Mohana-Borges

      Affiliations

    • Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Ilha do Fundão, 21941-590, Rio de Janeiro, RJ, Brazil
    • ,
  • Luís Maurício T.R. Lima

      Affiliations

    • Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, CCS, sala Bs-34, Ilha do Fundão, 21941-590, Rio de Janeiro, RJ, Brazil
    • Corresponding Author InformationCorresponding author. Fax: +55 21 2564 7380.

Received 10 January 2006; received in revised form 13 February 2006; accepted 17 February 2006. published online 23 February 2006.

Abstract 

The E2 proteins of papillomavirus specifically bind to double-stranded DNA containing the consensus sequence ACCG-N4-CGGT, where N is any nucleotide. Here, we show the binding and recognition of dissimilar DNA sequences by an 18 amino-acid peptide (α1E2), which corresponds to the DNA-recognition helix, α-helix-1. Isothermal DNA binding assays performed with the DNA consensus sequence show saturable curves with α1E2 peptide, and the α1E2 peptide is converted to an ordered conformation upon complexation. Measurements performed with non-specific DNA sequence fail to saturate, a behavior characteristic of non-specific binding. Binding of the α1E2 peptide to these DNA sequences display a different counter-ion dependence, indicating a dissimilar, sequence-dependent mechanism of interaction. Quantitative stoichiometric measurements revealed the specificity in α1E2 peptide recognition of the ACCG half-site, demonstrating capacity for discrimination of nucleic acid bases sequences without the need of a whole protein architecture.

Keywords: Peptide, DNA, Molecular recognition, Papillomavirus, E2 protein

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PII: S0014-5793(06)00248-1

doi:10.1016/j.febslet.2006.02.047

FEBS Letters
Volume 580, Issue 8 , Pages 1919-1924, 3 April 2006

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