Recognition of dual symmetry by the controller protein C.Esp1396I based on the structure of the transcriptional activation complex

DOI: 10.1093/nar/gkr1250

Authors: J. E. Mcgeehan (University of Portsmouth) , N. J. Ball (University of Portsmouth) , S. D. Streeter (University of Portsmouth) , S.-J. Thresh (University of Portsmouth) , G. G. Kneale (University of Portsmouth)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research , VOL 40 (9) , PAGES 4158-4167.

State: Published (Approved)
Published: December 2011

Abstract: The controller protein C.Esp1396I regulates the timing of gene expression of the restriction\u2013modifi- cation (RM) genes of the RM system Esp1396I. The molecular recognition of promoter sequences by such transcriptional regulators is poorly under- stood, in part because the DNA sequence motifs do not conform to a well-defined symmetry. We report here the crystal structure of the controller protein bound to a DNA operator site. The structure reveals how two different symmetries within the operator are simultaneously recognized by the homo-dimeric protein, underpinned by a conform- ational change in one of the protein subunits. The recognition of two different DNA symmetries through movement of a flexible loop in one of the protein subunits may represent a general mechan- ism for the recognition of pseudo-symmetric DNA sequences.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: ID14-1 at ESRF

Added On: 09/01/2012 14:24

Documents:
gkr1250.pdf

Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)