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

Wu, Jing; Beniac, Daniel R.; Harauz, George

doi:10.1007/bf00925923

Cited by 3 publications

(1 citation statement)

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“…The genome of T. lanuginosus , including those genes that encode ribosomal proteins, has not been fully sequenced to fully address this issue. Nonetheless, two-dimensional gel electrophoresis of T. lanuginosus 80S ribosomes revealed the same number, and similar size, of ribosomal proteins in both subunits as those in S. cerevisiae (Wu et al, 1995). Therefore, we believe the protein density relates to a ribosomal protein conserved throughout fungi and may become dissociated from the S. cerevisiae ribosome during purification while remaining bound to the T. lanuginosus ribosome.…”

Section: Resultsmentioning

confidence: 99%

Comprehensive Molecular Structure of the Eukaryotic Ribosome

et al. 2009

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Despite the emergence of a large number of X-ray crystallographic models of the bacterial 70S ribosome over the past decade, an accurate atomic model of the eukaryotic 80S ribosome is still not available. Eukaryotic ribosomes possess more ribosomal proteins and ribosomal RNA than bacterial ribosomes, which are implicated in extra-ribosomal functions in the eukaryotic cells. By combining cryo-EM with RNA and protein homology modeling, we obtained an atomic model of the yeast 80S ribosome complete with all ribosomal RNA expansion segments and all ribosomal proteins for which a structural homolog can be identified. Mutation or deletion of 80S ribosomal proteins can abrogate maturation of the ribosome, leading to several human diseases. We have localized one such protein unique to eukaryotes, rpS19e, whose mutations are associated with Diamond-Blackfan anemia in humans. Additionally, we characterize crucial and novel interactions between the dynamic stalk base of the ribosome with eukaryotic elongation factor 2.

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Section: Resultsmentioning

confidence: 99%

Comprehensive Molecular Structure of the Eukaryotic Ribosome

et al. 2009

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Structures of small subunit ribosomal RNAsin situ fromEscherichia coli andThermomyces lanuginosus

Beniac

Harauz

1995

Mol Cell Biochem

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Small ribosomal subunits from the prokaryote Escherichia coli and the eukaryote Thermomyces lanuginosus were imaged electron spectroscopically, and single particle analysis used to yield three-dimensional reconstructions of the net phosphorus distribution representing the nucleic acid (RNA) backbone. This direct approach showed both ribosomal RNAs to have a three domain structure and other characteristic morphological features. The eukaryotic small ribosomal subunit had a prominent bill present in the head domain, while the prokaryotic subunit had a small vestigial bill. Both ribosomal subunits contained a thick 'collar' central domain which correlates to the site of the evolutionarily conserved ribosomal RNA core, and the location of the majority of ribosomal RNA bases that have been implicated in translation. The reconstruction of the prokaryotic subunit had a prominent protrusion extending from the collar, forming a channel approximately 1.5 nm wide and potentially representing a 'bridge' to the large subunit in the intact monosome. The basal domain of the prokaryotic ribosomal subunit was protein free. In this region of the eukaryotic subunit, there were two basal lobes composed of ribosomal RNA, consistent with previous hypotheses that this is a site for the 'non-conserved core' ribosomal RNA.

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