Abstract:
:We have studied the structure of recombinant rat UBF (rrUBF), an RNA polymerase I transcription factor, by electron microscopy and image analysis of single particles contrasted with methylamine tungstate. Recombinant rat UBF appeared to be a flat, U-shaped protein with a central region of low density. In the dominant projections, 2-fold mirror symmetry was seen, consistent with the dimerization properties of this molecule, and of dimensions in agreement with the length of DNA that rat UBF protects in footprinting studies. Electron microscopy of various rrUBF-DNA complexes confirmed that our recombinant protein was fully able to bind the 45S rDNA promoter, and that it caused substantial bends in the DNA. Upon extended incubation in a droplet covered by a lipid monolayer at the liquid-air interface, rrUBF formed long filamentous arrays with a railway track appearance. This structure was interpreted to consist of overlapping rrUBF dimers 3.5 nm apart, which value would represent the thickness of the protein. Our results show rrUBF to interact with and bend the promoter DNA into a roughly 10 nm diameter superhelix. Based on all these electron microscopical results, an atomic structure was predicted by homology modelling of the HMG fingers, and connected by energy minimized intervening segments.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Neil KJ,Ridsdale RA,Rutherford B,Taylor L,Larson DE,Glibetic M,Rothblum LI,Harauz Gdoi
10.1093/nar/24.8.1472subject
Has Abstractpub_date
1996-04-15 00:00:00pages
1472-80issue
8eissn
0305-1048issn
1362-4962pii
6s0005journal_volume
24pub_type
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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pub_type: 杂志文章
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journal_title:Nucleic acids research
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journal_title:Nucleic acids research
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pub_type: 杂志文章
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