Inter-Protein Dependences During Assembly of the 50S Subunit from<i>Escherichia coli</i>Ribosomes

Röhl, Roland; Roth, Hans E.; Nierhaus, Knud H.

doi:10.1515/bchm2.1982.363.1.143

Cited by 8 publications

(4 citation statements)

References 16 publications

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“…In addition, quite a number of r-proteins are exclusively found either in bacteria or in eukaryotes [1], and together with species-specific variations in the primary structure of r-proteins and rRNA, these aspects could lead to differences in the intrinsic hierarchy of individual assembly events. Apart from this, yeast mutant studies resemble most likely in many cases “single omission” experiments while the assembly interrelationships in the LSU in vitro assembly maps were deduced from experiments involving a defined subset of r-proteins and rRNAs (see as example [107]). This reductionist approach could have led to the detection of assembly interrelationship not seen in vivo .…”

Section: Discussionmentioning

confidence: 99%

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Studies on the Assembly Characteristics of Large Subunit Ribosomal Proteins in S. cerevisae

et al. 2013

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During the assembly process of ribosomal subunits, their structural components, the ribosomal RNAs (rRNAs) and the ribosomal proteins (r-proteins) have to join together in a highly dynamic and defined manner to enable the efficient formation of functional ribosomes. In this work, the assembly of large ribosomal subunit (LSU) r-proteins from the eukaryote S. cerevisiae was systematically investigated. Groups of LSU r-proteins with specific assembly characteristics were detected by comparing the protein composition of affinity purified early, middle, late or mature LSU (precursor) particles by semi-quantitative mass spectrometry. The impact of yeast LSU r-proteins rpL25, rpL2, rpL43, and rpL21 on the composition of intermediate to late nuclear LSU precursors was analyzed in more detail. Effects of these proteins on the assembly states of other r-proteins and on the transient LSU precursor association of several ribosome biogenesis factors, including Nog2, Rsa4 and Nop53, are discussed.

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Section: Discussionmentioning

confidence: 99%

“…A good example for this is E. coli L5 (yeast rpL11) whose interaction with 23S rRNA was seen to depend in vitro on the presence of L2 (yeast rpL2) in an experimental setup including only L2, L5 and 23S rRNA [107]. Both E.…”

Section: Discussionmentioning

confidence: 99%

Studies on the Assembly Characteristics of Large Subunit Ribosomal Proteins in S. cerevisae

et al. 2013

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“…Both L4 and L22 have been associated with a group of 50S proteins involved in the peptidyl transferase center of the ribosome (Krayevsky, Kukhanova & Cohn, 1979). Binding interactions between these two proteins have been indicated previously (Rohl, Roth & Nierhaus, 1982;Roth & Nierhaus, 1980). Mutation-23 ally altered forms of L4 and L22 have been found in mutants of E. coli selected for high level resistance to erythromycin (Wittmann et al, 1973).…”

Section: Discussionmentioning

confidence: 94%

A temperature-sensitive mutant ofEscherichia coli with an alteration in ribosomal protein L22

Musich

1994

Genetica

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A temperature-sensitive, protein synthesis-defective mutant of Escherichia coli exhibiting an altered ribosomal protein L22 has been investigated. The temperature-sensitive mutation was mapped to the rplV gene for protein L22. The genes from the wild type and mutant strains were amplified by the polymerase chain reaction and the products were sequenced. A cytosine to thymine transition at position 22 of the coding sequence was found in the mutant DNA, predicting an arginine to cysteine alteration in the protein. A single cysteine residue was found in the isolated mutant protein. This amino acid change accounts for the altered mobility of the mutant protein in two-dimensional gels and during reversed-phase HPLC. The temperature-sensitive phenotype was fully complemented by a plasmid carrying the wild type L22 gene. Ribosomes from the complemented cells showed only wild type protein L22 by two dimensional gel analysis and were as heat-resistant as control ribosomes in a translation assay. The point mutation in the L22 gene is uniquely responsible for the temperature-sensitivity of this strain.

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“…This drastic conformational change can be demonstrated by biochemi cal and electron microscopical studies (Sieber et al 1980). The sequence in which the proteins bind to the RNA and the intermediate particles is depicted in the flow diagram (Dohme & Nierhaus 1976) and the assembly map (Roth et al 1980;Rohl et al 1982). As illustrated in the assembly map (figure 5) there are three assembly domains: the L20-domain, the L17-domain and the L15-domain.…”

Section: Reconstitutionmentioning

confidence: 97%

Review Lecture - Structure and evolution of ribosomes

Wittmann

1982

Proc. R. Soc. Lond. B.

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Ribosomes are the only cell organelles occurring in all organisms. E. coli ribosomes, which are the best characterized particles, consist of three RNAs and 53 proteins. All components have been isolated and characterized by chemical, physical and immunological methods. The primary structures of the RNAs and of all the proteins are known. Information about the secondary structure of the proteins derives from circular dichroism measurements and from secondary structure prediction methods. The tertiary structure is being studied by limited proteolysis, proton magnetic resonance and crystallization followed by X-ray analysis. Various methods are being used to elucidate the architecture of the ribosomal particle: three-dimensional image reconstruction of crystals of bacterial ribosomes and/or their subunits; immune electron microscopy; neutron scattering; protein-protein, protein-RNA and RNA‒RNA crosslinking; total reconstitution of ribosomal subunits. The results from these studies yield valuable information on the architecture of the ribosomal particle. Many mutants have been isolated in which one or a few ribosomal proteins are altered or even deleted. The genetic and biochemical characterization of these mutants allows conclusions about the importance of these proteins for the function of the ribosome. Ribosomal proteins from various prokaryotic and eukaryotic species have been compared by two-dimensional gel electrophoresis, immunological methods, reconstitution and amino acid sequence analysis. These studies show a strong homology among prokaryotic ribosomal proteins but only a weak homology between proteins from prokaryotic and eukaryotic ribosomes. Comparison of the primary and secondary structures of the ribosomal RNAs from various organisms shows that the secondary structure of the RNA molecules has been strongly conserved throughout evolution.

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Inter-Protein Dependences During Assembly of the 50S Subunit fromEscherichia coliRibosomes

Cited by 8 publications

References 16 publications

Studies on the Assembly Characteristics of Large Subunit Ribosomal Proteins in S. cerevisae

Studies on the Assembly Characteristics of Large Subunit Ribosomal Proteins in S. cerevisae

A temperature-sensitive mutant ofEscherichia coli with an alteration in ribosomal protein L22

Review Lecture - Structure and evolution of ribosomes

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