Electron microscopic visualisation of the 5S rRNA-YL3 complex from Saccharomyces cerevisiae

Kyle, Karen M.; Harauz, George

doi:10.1007/bf00230406

Mol Cell Biochem

1992

DOI: 10.1007/bf00230406

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Electron microscopic visualisation of the 5S rRNA-YL3 complex from Saccharomyces cerevisiae

Karen M. Kyle

George Harauz

Abstract: The complex comprising 5S ribosomal RNA and the ribosomal protein YL3 (5S rRNP) was isolated from yeast (Saccharomyces cerevisiae), and positively contrasted preparations were imaged by transmission electron microscopy. The overall dimensions of the 5S rRNP complex in the micrographs were 10 nm by 6 nm. Three predominant projections were selected from several hundred putative particles for digitisation and computer averaging to yield two-dimensional constructions with reproducible spatial resolutions exceeding… Show more

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Cited by 3 publications

References 38 publications

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Ribosomal proteins ofThermomyces lanuginosus ? characterisation by two-dimensional gel electrophoresis and differential disassembly

Beniac

Harauz

1995

Mol Cell Biochem

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One- and two-dimensional gel electrophoresis were employed to characterise the proteins derived from the ribosomes of the thermophilic fungus Thermomyces lanuginosus. Approximately 32 (29 basic and 3 acidic) and 45 (43 basic and 2 acidic) protein spots were resolved from Th. lanuginosus small and large ribosomal subunits, respectively. The molecular weight of the small subunit proteins ranged from 9,800-36,000 Da with a number average molecular weight of 20,300 Da. The molecular weight range for the large subunit proteins was 12,000-48,500 Da with a number average molecular weight of 25,900 Da. Most proteins appeared to be present in unimolar amounts. These data are comparable with but not identical to those from other eukaryotic ribosomes. The sensitivities of the ribosomal proteins to increasing concentrations of NH4Cl were also evaluated by two-dimensional gel electrophoresis. Most ribosomal proteins were gradually released over a wide range of salt concentrations but some were preferentially enriched in one or two salt conditions.

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Ribosomal proteins ofThermomyces lanuginosus ? characterisation by two-dimensional gel electrophoresis and differential disassembly

Beniac

Harauz

1995

Mol Cell Biochem

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A second-site mutation at glutamate-257 that restores the function of the mutant yeast ribosomal protein L5 containing lysine-270,271→arginine

Yeh¹,

Lee²

1999

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expres

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Structure of recombinant rat UBF by electron image analysis and homology modelling

Neil

Ridsdale

Rutherford

et al. 1996

Nucleic Acids Research

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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.

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Electron microscopic visualisation of the 5S rRNA-YL3 complex from Saccharomyces cerevisiae

Cited by 3 publications

References 38 publications

Ribosomal proteins ofThermomyces lanuginosus ? characterisation by two-dimensional gel electrophoresis and differential disassembly

Ribosomal proteins ofThermomyces lanuginosus ? characterisation by two-dimensional gel electrophoresis and differential disassembly

A second-site mutation at glutamate-257 that restores the function of the mutant yeast ribosomal protein L5 containing lysine-270,271→arginine

Structure of recombinant rat UBF by electron image analysis and homology modelling

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