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Science 20 May 1994:
Vol. 264. no. 5162, pp. 1134 - 1137
DOI: 10.1126/science.8178172
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Articles

Science, Vol 264, Issue 5162, 1134-1137
Copyright © 1994 by American Association for the Advancement of Science

articles

Short-range DNA looping by the Xenopus HMG-box transcription factor, xUBF

DP Bazett-Jones, B Leblanc, M Herfort, and T Moss

Department of Medical Biochemistry and Anatomy, Faculty of Medicine, Health Sciences Center, University of Calgary, Alberta, Canada.

Xenopus UBF (xUBF) interacts with DNA by way of multiple HMG-box domains. When xUBF binds to the ribosomal promoter, the carboxyl-terminal acidic tail and amino-terminal HMG-box interact. Binding also leads to negative DNA supercoiling and the formation of a disk-like structure, the enhancesome. Within the enhancesome, an xUBF dimer makes a low-density protein core around which DNA is looped into a single 180-base pair turn, probably by in-phase bending. The enhancesome structure suggests a mechanism for xUBF-dependent recruitment of the TATA box-binding protein complex without direct interaction between the two factors.


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