Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach

Nucleic Acids Res. 2007;35(10):e75. doi: 10.1093/nar/gkm040. Epub 2007 May 8.

Abstract

We have developed a novel DNA microarray-based approach for identification of the sequence-specificity of single-stranded nucleic-acid-binding proteins (SNABPs). For verification, we have shown that the major cold shock protein (CspB) from Bacillus subtilis binds with high affinity to pyrimidine-rich sequences, with a binding preference for the consensus sequence, 5'-GTCTTTG/T-3'. The sequence was modelled onto the known structure of CspB and a cytosine-binding pocket was identified, which explains the strong preference for a cytosine base at position 3. This microarray method offers a rapid high-throughput approach for determining the specificity and strength of ss DNA-protein interactions. Further screening of this newly emerging family of transcription factors will help provide an insight into their cellular function.

Publication types

  • Research Support, Non-U.S. Gov't
  • Validation Study

MeSH terms

  • Archaeal Proteins / metabolism
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Binding Sites
  • Binding, Competitive
  • Calorimetry
  • Carbocyanines
  • Consensus Sequence
  • Cytosine / chemistry
  • DNA, Single-Stranded / chemistry
  • DNA, Single-Stranded / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Electrophoretic Mobility Shift Assay
  • Fluorescent Dyes
  • Heat-Shock Proteins / metabolism
  • Models, Molecular
  • Oligonucleotide Array Sequence Analysis / methods*

Substances

  • Archaeal Proteins
  • Bacterial Proteins
  • Carbocyanines
  • DNA, Single-Stranded
  • DNA-Binding Proteins
  • Fluorescent Dyes
  • Heat-Shock Proteins
  • cold shock protein, Bacillus
  • cyanine dye 5
  • Cytosine