PMID:17088256
| Citation |
Johnston, D, Tavano, C, Wickner, S and Trun, N (2006) Specificity of DNA binding and dimerization by CspE from Escherichia coli. J. Biol. Chem. 281:40208-15 |
|---|---|
| Abstract |
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 (K(D) < 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. |
| Links |
PubMed Online version:10.1074/jbc.M606414200 |
| Keywords |
Amino Acid Sequence; Chromatography, Gel; Chromosomes, Bacterial/chemistry; Chromosomes, Bacterial/metabolism; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; DNA, Single-Stranded/chemistry; DNA, Single-Stranded/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Dimerization; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Molecular Sequence Data |
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