Interaction of a tryptophan‐containing peptide with chromatin core particles

FEBS Letters

Colot, Vincent²  Helene, Claude¹  Toulme, Jean-Jacques¹ 

[1] Laboraoire de Biophysique, INSERM U 201, CNRS ERA 951, Muséum National d'Histoire Naturelle, 61, Rue Buffon, 75005 Paris, France;Laboratoire de Technologie des Céréales, INRA, 9, Place Viala, 34060 Montpellier Cédex, France

关键词: Peptide—DNA complex;    Stacking interaction;    Core particle;    Fluorescence;   

DOI  :  10.1016/0014-5793(84)80319-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The binding of a tetrapeptide lysyltryptophylglycyllysine to nucleosome core particles has been investigated using UV absorption and fluorescence spectroscopy. Modifications of the absorption spectra and fluorescence quenching of the tryptophyl residue are consistent with stacking between the indole ring and nucleic acid bases. Therefore DNA interactions with histones do not prevent stacking of the tryptophyl residue with nucleic acid bases in the peptide—core particle complexes. The number of peptide binding sites is reduced to half that of naked DNA.

【 授权许可】

Unknown