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Title: Oligomerization and DNA binding of Ler, a master regulator of pathogenicity of enterohemorrhagic and enteropathogenic Escherichia coli
Author: García, Jesús
Cordeiro, Tiago N.
Prieto, Maria J.
Pons Vallès, Miquel
Keywords: Regulació genètica
Àcids nucleics
Genetic regulation
Nucleic acids
Issue Date: 1-Nov-2012
Publisher: Oxford University Press
Abstract: Ler is a DNA-binding, oligomerizable protein that regulates pathogenicity islands in enterohemorrhagic and enteropathogenic Escherichia coli strains. Ler counteracts the transcriptional silencing effect of H-NS, another oligomerizable nucleoid-associated protein. We studied the oligomerization of Ler in the absence and presence of DNA by atomic force microscopy. Ler forms compact particles with a multimodal size distribution corresponding to multiples of 3-5 units of Ler. DNA wraps around Ler particles that contain more than 15-16 Ler monomers. The resulting shortening of the DNA contour length is in agreement with previous measurements of the length of DNA protected by Ler in footprinting assays. We propose that the repetition unit corresponds to the number of monomers per turn of a tight helical Ler oligomer. While the repressor (H-NS) and anti-repressor (Ler) have similar DNA-binding domains, their oligomerization domains are unrelated. We suggest that the different oligomerization behavior of the two proteins explains the opposite results of their interaction with the same or proximal regions of DNA.
Note: Reproducció del document publicat a:
It is part of: Nucleic Acids Research, 2012, vol. 40, num. 20, p. 10254-10262
ISSN: 0305-1048
Appears in Collections:Publicacions de projectes de recerca finançats per la UE
Articles publicats en revistes (Química Inorgànica i Orgànica)

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