期刊论文详细信息
FEBS Letters | |
Cooperative and salt‐resistant binding of LexA protein to non‐operator DNA | |
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
【 预 览 】
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