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

作者信息

Lukiw W J, Kruck T P, McLachlan D R

机构信息

Collaborative Program in Neuroscience, University of Toronto, Canada.

出版信息

FEBS Lett. 1989 Aug 14;253(1-2):59-62. doi: 10.1016/0014-5793(89)80929-9.

DOI:10.1016/0014-5793(89)80929-9
PMID:2759243
Abstract

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.

摘要

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