| Literature DB >> 8178172 |
D P Bazett-Jones1, B Leblanc, M Herfort, T Moss.
Abstract
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.Entities:
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Year: 1994 PMID: 8178172 DOI: 10.1126/science.8178172
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728