Nucleic Acids Research, Vol 26, Issue 11 2580-2585, Copyright © 1998 by Oxford University Press
T Yoshima, T Yura and H Yanagi
DNA binding of heat shock factor 2 (HSF2) is induced during hemin- induced
differentiation of human erythroleukemia cell line K562. To identify the
transcriptional activation and the regulatory domains of HSF2, we
constructed a series of deletion derivatives fused to the yeast GAL4 DNA
binding domain and analyzed their transactivation activity. A minimal
transactivation domain of HSF2 was localized to the C-terminus (residues
472-536), as in HSF1, although amino acid sequence similarity for these
regions was rather limited and the potential transactivation ability was
about 25% that of HSF1. The transactivation mediated by this region of HSF2
was found to be negatively regulated by the adjacent 18 amino acid segment
(residues 428-445) under normal conditions. Furthermore, the latter
segment, when fused to the GAL4 activation domain, markedly inhibited GAL4
activity. Extract containing most derivatives of HSF2 retaining this
segment exhibited doublet or triplet bands in gel mobility shift assays
with heat shock element- containing DNA, suggesting possible involvement of
some factors interacting with that segment in the negative regulation.
Another putative transactivation domain and two negative regulatory regions
were also localized within the internal region.
ARTICLES
Function of the C-terminal transactivation domain of human heat shock factor 2 is modulated by the adjacent negative regulatory segment
HSP Research Institute, Kyoto Research Park, Shimogyo-ku, Kyoto 600- 8813, Japan.
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