Cooperative and salt-resistant binding of LexA protein to non-operator DNA
- 11 June 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 171 (2), 207-210
- https://doi.org/10.1016/0014-5793(84)80489-5
Abstract
The interaction of the lexA repressor of E. coli with poly[d(A‐T)] has been studied by circular dichroism. The binding induces an about 2‐fold increase of the circular dichroism intensity at 263 nm, pointing out a conformational change of the nucleic acid. The observed spectral changes are very similar to those observed for the binding of the lac repressor to poly[d(A‐T)] and natural DNA. At elevated ionic strength the binding isotherms do show a pronounced sigmoidal shape indicating a cooperative mode of binding.Keywords
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