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Linker histone‐DNA complexes: enhanced stability in the presence of aluminum lactate and implications for Alzheimer's disease
Author(s) -
Lukiw W.J.,
Kruck T.P.A.,
McLachlan D.R.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80929-9
Subject(s) - linker , linker dna , histone , chemistry , dna , biochemistry , biophysics , sodium , histone h1 , biology , organic chemistry , computer science , operating system
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.