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BvgA and RNA polymerase alpha subunit bind to different faces of DNA.
2003 APR 2 - (NewsRx.com & NewsRx.net) -- The response regulator BvgA and RNA polymerase alpha subunit C-terminal domain bind simultaneously to different faces of the same segment of promoter DNA.
"Examination of the binding of FeBABE-conjugated BvgA to the fha promoter of Bordetella pertussis has revealed that three dimers, formed by head-to-head association of monomers, bind one face of the DNA helix from the inverted-heptad primary binding site to the -35 region," researchers in the United States report.
"The orientation of BvgA monomers within the dimers is the same as that recently demonstrated by X-ray crystallographic methods for a dimer of the C-terminal domain of NarL bound to DNA," said Philip E. Boucher and colleagues at the Food and Drug Administration and the University of California-Los Angeles. "Use of FeBABE conjugates of RNAP alpha subunit C-terminal domain showed that binding of this domain is linearly coincident with binding of the BvgA dimers, but to a different helical face."
The researchers concluded, ...
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