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Nucleic Acids Research, 2001, Vol. 29, No. 15 3241-3247
© 2001 Oxford University Press

DNA looping in the RNA polymerase I enhancesome is the result of non-cooperative in-phase bending by two UBF molecules

Victor Y. Stefanovsky, Guillaume Pelletier, David P. Bazett-Jones1, Colyn Crane-Robinson2 and Tom Moss*

Cancer Research Centre and Department of Medical Biology, Laval University, Hôtel-Dieu de Québec, 11 Côte du Palais, Québec G1R 2J6, Canada, 1Department of Cell Biology and Anatomy, Faculty of Medicine, Health Sciences Center, University of Calgary, Alberta T2N 4N1, Canada and 2Biophysics Laboratories, University of Portsmouth, St Michael’s Building, White Swan Road, Portsmouth, UK

The so-called upstream binding factor (UBF) is required for the initial step in formation of an RNA polymerase I initiation complex. This function of UBF correlates with its ability to induce the ribosomal enhancesome, a structure which resembles in its mass and DNA content the nucleosome of chromatin. DNA looping in the enhancesome is probably the result of six in-phase bends induced by the HMG boxes of a UBF dimer. Here we show that insertion/deletion mutations in the basic peptide linker lying between the N-terminal dimerisation domain and the first HMG box of Xenopus UBF prevent the DNA looping characteristic of the enhancesome. Using these mutants we demonstrate that (i) the enhancesome structure does not depend on tethering of the entering and exiting DNA duplexes, (ii) UBF monomers induce hemi-enhancesomes, bending the DNA by 175 ± 24° and (iii) two hemi-enhancesomes are precisely phased by UBF dimerisation. We use this and previous data to refine the existing enhancesome model and show that HMG boxes 1 and 2 of UBF lie head-to-head along the DNA.

* To whom correspondence should be addressed. Tel: +1 418 525 4444; Fax: +1 418 691 5439; Email: tom.moss{at}crhdq.ulaval.ca


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