Nucleic Acids Research, Vol 24, Issue 23 4733-4740, Copyright © 1996 by Oxford University Press
T Suda, Y Mishima, K Takayanagi, H Asakura, S Odani and R Kominami
The high mobility group protein (HMG)-box is a DNA-binding domain found in
many proteins that bind preferentially to DNA of irregular structures in a
sequence-independent manner and can bend the DNA. We show here that
GST-fusion proteins of HMG domains from HMG1 and HMG2 promote a
triple-stranded complex formation between DNA containing the (GGA/TCC)11
repeat and oligonucleotides of d(GGA)11 probably due to G:G base pairing.
The activity is to reduce association time and requirements of Mg2+ and
oligonucleotide concentrations. The HMG box of SRY, the protein determining
male-sex differentiation, also has the activity, suggesting that it is not
restricted to the HMG-box domains derived from HMG1/2 but is common to
those from other members of the HMG-box family of proteins. Interestingly,
the box-AB and box-B of HMG1 bend DNA containing the repeat, but SRY fails
to bend in a circularization assay. The difference suggests that the two
activities of association-promotion and DNA bending are distinct. These
results suggest that the HMG-box domain has a novel activity of promoting
the association between GGA repeats which might be involved in higher-order
architecture of chromatin.
ARTICLES
A novel activity of HMG domains: promotion of the triple-stranded complex formation between DNA containing (GGA/TCC)11 and d(GGA)11 oligonucleotides
First Department of Biochemistry, Niigata University School of Medicine, Japan.
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