Flexing DNA: HMG-Box Proteins and Their Partners

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Flexing DNA: HMG-Box Proteins and Their Partners Marco E. Bianchi, Monica Beltrame The American Journal of Human Genetics Volume 63, Issue 6, Pages 1573-1577 (December 1998) DOI: 10.1086/302170 Copyright © 1998 The American Society of Human Genetics Terms and Conditions

Figure 1 Structure of the complex between the HMG box of human SRY and the octanucleotide GCACAAAC. HMG boxes are composed of three α-helices and an extended amino acid stretch at their N-terminus. The Cα backbone of the SRY HMG-box (magenta) is almost exactly superimposable upon that of HMG boxes from mammalian HMG1 and Drosophila HMG-D, which share only ∼20% identity in primary sequence. The DNA (yellow) is significantly distorted: the minor groove is widened considerably to accommodate the extended stretch of the HMG box; the planes of the bases are tilted; and the double helix is unwound and bent. Very similar features are also present in DNA complexed to TBP, which also binds via the minor groove but which has a completely different protein fold. The contact between the HMG box and the DNA occurs over a surprisingly large area and with a very tight fit; thus, the energetic cost of distorting the DNA is more than compensated by the chemical energy freed by the protein-DNA interaction. This model is derived from the atomic coordinates provided by Werner et al. (1995). The American Journal of Human Genetics 1998 63, 1573-1577DOI: (10.1086/302170) Copyright © 1998 The American Society of Human Genetics Terms and Conditions

Figure 2 Model for the action of SRY and other HMG-box proteins. An HMG-box protein (orange) such as SRY binds to target DNA sequences, which it bends considerably. The angle in the DNA depicted here approximates that caused by SRY. The flexure of the DNA brings proteins (blue and green) bound to each side of the site into proximity, thus promoting their interaction. The presence of contact surfaces between SRY and one or both neighboring proteins may stabilize the whole complex and increase its target specificity. The same model can apply to HMG1. HMG1 binds to DNA regardless of sequence, so protein-protein interactions with partners are essential to direct it to the DNA sites where flexing is to occur. The American Journal of Human Genetics 1998 63, 1573-1577DOI: (10.1086/302170) Copyright © 1998 The American Society of Human Genetics Terms and Conditions