DNA recognition of a 24-mer peptide derived from RecA protein

Biopolymers. 2000;55(6):416-24. doi: 10.1002/1097-0282(2000)55:6<416::AID-BIP1017>3.0.CO;2-P.

Abstract

A novel 24-residue peptide (L2-G), Ile-Arg-Met-Lys-Ile-Gly-Val-Met-Phe-Gly-Asn-Pro-Glu-Thr-Thr-Thr-Gly-Gly-Asn-Ala-Leu-Lys-Phe-Tyr, derived from RecA can discriminate a single-stranded DNA (ssDNA) from a double-stranded DNA (dsDNA) and a new developed support with this peptide recognizes not dsDNA but ssDNA. The 24-mer peptide with L2 and helix G amino acids of Escherichia coli RecA protein showed the ssDNA binding property with more than 1000 times affinity difference for the dsDNA. However, truncated 15-mer peptide showed no ssDNA binding activity. In the ssDNA binding, L2-G changed its conformation with the perturbation of an alpha-helix structure. The ssDNA binding and the DNA discrimination property of this peptide were due to almost all L2 and helix G amino acids, respectively. This result is useful to design synthetic peptides as functional materials for DNA recognition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Chromatography, Affinity
  • Circular Dichroism
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Molecular Sequence Data
  • Molecular Structure
  • Nucleic Acid Conformation
  • Peptides / chemical synthesis
  • Peptides / chemistry
  • Peptides / metabolism*
  • Protein Binding
  • Protein Conformation
  • Rec A Recombinases / chemistry
  • Rec A Recombinases / genetics
  • Rec A Recombinases / metabolism*

Substances

  • DNA-Binding Proteins
  • Peptides
  • DNA
  • Rec A Recombinases