Cooperative and salt‐resistant binding of LexA protein to non‐operator DNA | Zendy

Schnarr Manfred | Zendy; Daune Michel | Zendy

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Cooperative and salt‐resistant binding of LexA protein to non‐operator DNA

Author(s) -

Schnarr Manfred,

Daune Michel

Publication year - 1984

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/0014-5793(84)80489-5

Subject(s) - repressor lexa , circular dichroism , repressor , dna , chemistry , ionic strength , lac repressor , biophysics , conformational change , nucleic acid , biochemistry , crystallography , stereochemistry , biology , gene , transcription factor , aqueous solution

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.

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