PMID: 8972860Dec 1, 1996Paper

A novel activity of HMG domains: promotion of the triple-stranded complex formation between DNA containing (GGA/TCC)11 and d(GGA)11 oligonucleotides

Nucleic Acids Research
T SudaR Kominami

Abstract

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.

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Citations

Jun 12, 2003·Developmental Biology·Jennifer Schmahl, Blanche Capel
May 23, 2002·DNA and Cell Biology·Guohong LiPeter Traub
Jan 10, 2002·Biochemical and Biophysical Research Communications·Akira YoshimuraYukio Mishima
Apr 20, 2011·Biochimie·Anirban Mukherjee, Karen M Vasquez
Apr 29, 2011·RNA Biology·Fabian A BuskeTimothy L Bailey
Apr 12, 2021·Biochemical and Biophysical Research Communications·Koji KatsumataMitsuhiro Shimizu

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