Linker histone-DNA complexes: enhanced stability in the presence of aluminum lactate and implications for Alzheimer's disease.
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(0) 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.
Collaborative Program in Neuroscience, University of Toronto, Canada.
W J
WJ
Lukiw
T P
TP
Kruck
D R
DR
McLachlan
D000544:Alzheimer Disease / Q000503:physiopathology*; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007773:Lactates / Q000494:pharmacology*; D019344:Lactic Acid; D011485:Protein Binding / Q000187:drug effects; D012091:Repetitive Sequences, Nucleic Acid; D012965:Sodium Chloride / Q000494:pharmacology
D004268:DNA-Binding Proteins; D006657:Histones; D007773:Lactates; D019344:Lactic Acid; D012965:Sodium Chloride; D004247:DNA