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

FEBS Letters

Schnarr, Manfred¹  Daune, Michel¹ 

[1] Institut de Biologie Moléculaire et Cellulaire du CNRS, Laboratoire de Biophysique, 15 rue René Descartes, 67084 Strasbourg Cédex, France

关键词: SOS response;    lexA repressor;    Protein—nucleic acid interaction;    Cooperativity;    Circular dichroism;   

DOI  :  10.1016/0014-5793(84)80489-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown