Interference of AlF4- with nucleotide and DNA binding of rat histone H1 in vitro. Implications for the pathogenesis of Alzheimer's disease.
We demonstrate here that the H2PO4- analogue AlF4- binds to the nucleotide-binding site of rat liver histone H1 in vitro, and interferes with nucleotide recognition and H1 DNA binding. AlF4- may thus compromise the genetically determined pattern of protein synthesis through binding to H1, the general repressor. The present findings are of interest as a number of studies have implicated aluminium as a factor in the pathogenesis of Alzheimer's disease.
Oikarinen
J
J
Collagen Research Unit, University of Oulu, Finland.
Mannermaa
R M
RM
Tarkka
T
T
Yli-Mäyry
N
N
Majamaa
K
K
D000535:Aluminum / Q000494:pharmacology*; D017607:Aluminum Compounds; D000544:Alzheimer Disease / Q000209:etiology*; D000818:Animals; D001665:Binding Sites; D004247:DNA / Q000378:metabolism*; D005459:Fluorides; D005461:Fluorine / Q000494:pharmacology*; D006657:Histones / Q000378:metabolism*; D008099:Liver / Q000378:metabolism; D009711:Nucleotides / Q000378:metabolism*; D051381:Rats
D017607:Aluminum Compounds; D006657:Histones; D009711:Nucleotides; C050992:tetrafluoroaluminate; D005461:Fluorine; D004247:DNA; D000535:Aluminum; D005459:Fluorides