Zinc is required for folding and binding of a single zinc finger to DNA

FEBS Letters

Lee, Min S.²  Gottesfeld, Joel M.¹  Wright, Peter E.² 

[1] Department of Molecular Biology, Medical Biology Institute, La Jolla, CA 92037, USA;Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037, USA

关键词: Zinc finger;    DNA-binding;    2D NMR;    NOE;    nuclear Overhauser effect;    NOESY;    nuclear Overhauser effect spectroscopy;    COSY;    scalar correlated spectroscopy;   

DOI  :  10.1016/0014-5793(91)80170-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A synthetic peptide corresponding to zinc finger 31 of the Xenopus protein adopts a folded conformation in the presence of zinc. The same peptide in the absence of zinc is not folded in a stable tertiary conformation, as determined by NMR. Binding experiments have shown that the peptide binds non-specifically to DNA only in the presence of zinc. Moreover, competive DNA binding experiments indicate interaction with 3.9 ± base pairs.

【 授权许可】

Unknown