Specificity of DNA binding and dimerization by CspE from Escherichia coli
Journal of Biological Chemistry
The CspE protein from Escherichia coli K12 is a single-stranded nucleic acid-binding protein that plays a role in chromosome condensation in vivo. We report here that CspE binds to single-stranded DNA containing 6 or more contiguous dT residues with high affinity (KD < 30 nM). The interactions are predominantly through base-specific contacts. When an oligonucleotide contains fewer than 6 contiguous dT residues, the CspE interactions with single-stranded DNA are primarily electrostatic. The minimal length of single-stranded DNA to which CspE binds in a salt-resistant manner is eight nucleotides. We also show that CspE exists as a dimer in solution. We present a possible mechanism to explain the role of CspE in chromosome condensation in vivo by CspE binding to distant DNA regions in the chromosome and dimerizing, thereby condensing the intervening DNA.
Johnston, D., Tavano, C., Wickner, S., & Trun, N. (2006). Specificity of DNA binding and dimerization by CspE from Escherichia coli. Journal of Biological Chemistry, 281 (52), 40208-40215. https://doi.org/10.1074/jbc.M606414200