Linker histone‐DNA complexes: enhanced stability in the presence of aluminum lactate and implications for Alzheimer's disease

FEBS Letters

McLachlan, D.R.²  Kruck, T.P.A.²  Lukiw, W.J.¹ 

[1] Collaborative Program in Neuroscience, Medical Sciences Building, University of Toronto, Toronto M5S IA8, Canada;Center for Research in Neurodegenerative Disease, Medical Sciences Building, University of Toronto, Toronto M5S IA8, Canada

关键词: Linker histone;    Histone H1°;    Alu repetitive element;    Chromatin structure;    Aluminum neurotoxicity;    Alzheimer's disease;    (Brain);    TGSDS-PAGE;    Tris-glycine-SDS-poly-acrylamide gel electrophoresis;    PCA;    perchloric acid;    TAE;    Tris-acetate-EDTA;    LMG;    low mobility group;    A;    adenine;    T;    thymine;    BRL;    Bethesda Research Laboratories;   

DOI  :  10.1016/0014-5793(89)80929-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The binding of human brain linker histone proteins to a radiolabelled human Alu repetitive element was examined by mobility shift assay.. Analysis of the complexes formed from protein extracts of whole neocortical nuclei, under physiological conditions in vitro revealed that linker histone H1° has the highest affinity for the Alu DNA sequence. The linker histone-DNA complexes assembled in the presence of aluminum lactate were more resistant to sodium chloride-induced dissociation than those formed in the presence of sodium lactate. The enhanced stability of deoxyribonucleoprotein (DNP) complexes in the presence of the aluminum cation may be of significance in neurodegenerative conditions such as Alzheimer's disease where aluminum preferentially associates with DNA containing structures of the nucleus.

【 授权许可】

Unknown