H-1, C-13, and N-15 Resonance Assignments of the DNA Binding Domain of Ler from Enteropathogenic E. coli in Complex with DNA

Ler is a master regulator for the gene regulation of the locus of enterocyte effacement (LEE) pathogenicity island (PAI), which could activate the transcription of LEE2 to LEE5 by counteracting the repression of H-NS. Ler contains an N-terminal oligomerization domain, a linker region, and a C-terminal DNA binding domain. However, the DNA binding mechanism of Ler remains unclear. Here, we report the H-1, C-13, and N-15 NMR assignments of Ler(CTD)/3A3T-DNA complex. We have achieved 97.8% completeness for the backbone and side-chain resonance assignments of Ler(CTD) in the complex, excluding C-13 & PRIME; resonances. In addition, about 91.5% of the H-1 resonances of 3A3T-DNA have been assigned. Our near complete assignments of this complex will significantly advance the parsing of the intermolecular NOE signals between Ler (CTD) and 3A3T-DNA. Therefore, our NMR assignments formed a good basis for further DNA binding mechanism studies of Ler.