A NMR guided approach for CsrA-RNA crystallization

J Biomol NMR. 2013 May;56(1):31-9. doi: 10.1007/s10858-013-9712-3. Epub 2013 Jan 29.

Abstract

Structure determination of protein-nucleic acid complexes remains a challenging task. Here we present a simple method for generating crystals of a CsrA-nucleic acid complex, guided entirely by results from nuclear magnetic resonances spectroscopy (NMR) spectroscopy. Using a construct that lacks thirteen non-essential C-terminal residues, efficient binding to DNA could be demonstrated. One CsrA dimer interacts with two DNA oligonucleotides, similar to previous findings with RNA. Furthermore, the NMR study of the CsrA-DNA complex was the basis for successfully homing in on conditions that were suitable for obtaining crystals of the CsrA-DNA complex. Our results may be useful for those cases where RNA in protein-nucleic acid complexes may be replaced by DNA.

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / genetics
  • Bacillus subtilis / metabolism*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Base Sequence
  • Binding Sites / genetics
  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA / metabolism
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular*
  • Nucleic Acid Conformation
  • Protein Multimerization / physiology
  • RNA / chemistry*
  • RNA / metabolism
  • RNA-Binding Proteins / chemistry
  • RNA-Binding Proteins / metabolism
  • Repressor Proteins / chemistry
  • Repressor Proteins / metabolism
  • Sequence Homology, Amino Acid
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism

Substances

  • Bacterial Proteins
  • CsrA protein, E coli
  • Escherichia coli Proteins
  • RNA-Binding Proteins
  • Repressor Proteins
  • Transcription Factors
  • RNA
  • DNA