DNA tape measurements of AraC.
A new method for measuring distances between points in the AraC-DNA complex was developed and applied. It utilizes variable lengths of single-stranded DNA that connect double-stranded regions containing the two half-site binding sequences of AraC. These distances plus the protein interdomain linker distances are compatible with two classes of structure for the dimeric AraC gene regulatory protein. In one class, the N-terminal regulatory arm of one dimerization domain is capable of interacting with the DNA-binding domain on the same polypeptide chain for a cis interaction. In the other class, the possible arm-DNA-binding domain interaction is trans, where it adds to the dimerization interface.
Rodgers
Michael E
ME
Biology Department, Johns Hopkins University, 3400 N. Charles St, Baltimore, MD 21218, USA.
Schleif
Robert
R
D051777:AraC Transcription Factor / Q000737:chemistry* / Q000378:metabolism; D001089:Arabinose / Q000378:metabolism; D001665:Binding Sites; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000737:chemistry / Q000378:metabolism; D019281:Dimerization; D024202:Electrophoretic Mobility Shift Assay; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D051777:AraC Transcription Factor; C497371:AraC protein, E coli; D004277:DNA, Single-Stranded; D029968:Escherichia coli Proteins; D004247:DNA; D001089:Arabinose