Nucleic Acids Research, Vol 24, Issue 15 2959-2965, Copyright © 1996 by Oxford University Press
H Maeshima, M Sato, K Ishikawa, Y Katagata and T Yoshida
We have reported that an upstream stimulatory factor (USF) binding site is
functional in transcription of the heme oxygenase-1 gene. In this study, we
examined the role of USF in the induced state. By transient expression
analyses with the chloramphenicol acetyl-transferase gene, we found that
the USF binding site plays an important role in the induction of rat heme
oxygenase-1 by cadmium, but not by hemin. To elucidate the role of USF, we
prepared USF-rich nuclear extracts from control and cadmium-treated rat
liver. On electrophoretic mobility shift assay using control nuclear
proteins, one slowly migrating band was detected, whereas using nuclear
proteins of cadmium-treated rat liver, two fast migrating bands were
detected. The molecular masses of the two subunits of USF prepared from
cadmium-treated rat liver were approximately 34 kDa as determined by UV
cross-linking and subsequent SDS-PAGE, while the two subunits of native USF
were 43 kDa and 44 kDa. DNase I footprinting analysis revealed that both
the nuclear proteins bound to the same region including the USF binding
site. We therefore suppose that cadmium causes some structural changes in
the two proteins of USF and that the altered USF participates in the
effective initiation of transcription of the rat heme oxygenase-1 gene.
ARTICLES
Participation of altered upstream stimulatory factor in the induction of rat heme oxygenase-1 by cadmium
Department of Biochemistry, Central Laboratory for Research and Education, Yamagata University School of Medicine, Japan.
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