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Titolo:
STRUCTURE OF RECOMBINANT RAT UBF BY ELECTRON IMAGE-ANALYSIS AND HOMOLOGY MODELING
Autore:
NEIL KJ; RIDSDALE RA; RUTHERFORD B; TAYLOR L; LARSON DE; GLIBETIC M; ROTHBLUM LI; HARAUZ G;
Indirizzi:
UNIV GUELPH,DEPT MOLEC BIOL & GENET GUELPH ON N1G 2W1 CANADA UNIV GUELPH,DEPT MOLEC BIOL & GENET GUELPH ON N1G 2W1 CANADA ONTARIO CANC INST TORONTO ON M5G 2M9 CANADA WEIS CTR RES,GEISINGER CLIN DANVILLE PA 17822
Titolo Testata:
Nucleic acids research
fascicolo: 8, volume: 24, anno: 1996,
pagine: 1472 - 1480
SICI:
0305-1048(1996)24:8<1472:SORRUB>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA POLYMERASE-I; TATA-BINDING PROTEIN; TRANSCRIPTION FACTOR UBF; DNA-BINDING; SINGLE PARTICLES; INITIATION SITE; RIBOSOMAL DNA; FACTOR XUBF; MICROSCOPY; PROMOTER;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
67
Recensione:
Indirizzi per estratti:
Citazione:
K.J. Neil et al., "STRUCTURE OF RECOMBINANT RAT UBF BY ELECTRON IMAGE-ANALYSIS AND HOMOLOGY MODELING", Nucleic acids research, 24(8), 1996, pp. 1472-1480

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 centralregion 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 ratUBF 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 lipidmonolayer at the liquid-air interface, rrUBF formed long filamentous arrays with a railway track appearance. This structure was interpretedto consist of overlapping rrUBF dimers 3.5 nm apart, which value would represent the thick ness 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 09:04:25