Yeast ribosomal proteins: V. Correlation of several nomenclatures and proposal of a standard nomenclature

Otaka, Eiko; Osawa, Syozo

doi:10.1007/bf00268424

Cited by 77 publications

(27 citation statements)

References 16 publications

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“…Yeast transformation was performed by the lithium acetate procedure (4 ORF interrupted by an intron. The possibility that the ORF (SWISS-PROT), was confirmed by the fact that when the encoded a protein homologous to the L41 (5) (also called ORF sequence prepared by removing an intron from the YP44 or YL27 [11]) protein of the 60S ribosomal subunit of RIM-C gene was inserted alone into a YEp-type expression S. cerevisiae, suggested from a search of a protein data base vector, pAAH5, the recombinant plasmid conferred resis- tance to 100 ,ug of CYH per ml on S. cerevisiae (data not (8). A genomic library from S. cerevisiae AH22 containing shown).…”

Section: Methodsmentioning

confidence: 99%

Drastic alteration of cycloheximide sensitivity by substitution of one amino acid in the L41 ribosomal protein of yeasts

et al. 1992

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Cycloheximide is one of the antibiotics that inhibit protein synthesis in most eukaryotic cells. We have found that a yeast, Candida maltosa, is resistant to the drug because it possesses a cycloheximide-resistant ribosome, and we have isolated the gene responsible for this. In this study, we sequenced this gene and found that the gene encodes a protein homologous to the L41 ribosomal protein of Saccharomyces cerevisiae, whose amino acid sequence has already been reported. Two genes for L41 protein, named L41a and L41b, independently present in the genome of S. cerevisiae, were isolated. L41-related genes were also isolated from a few other yeast species. Each of these genes has an intron at the same site of the open reading frame. Comparison of their deduced amino acid sequences and their ability to confer cycloheximide resistance to S. cerevisiae, when introduced in a high-copy-number plasmid, suggested that the 56th amino acid residue of the L41 protein determines the sensitivity of the ribosome to cycloheximide; the amino acid is glutamine in the resistant ribosome, whereas that in the sensitive ribosome is proline. This was confirmed by constructing a cycloheximide-resistant strain of S. cerevisiae having a disrupted L41a gene and an L41b gene with a substitution of the glutamine codon for the proline codon.

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Section: Methodsmentioning

confidence: 99%

Drastic alteration of cycloheximide sensitivity by substitution of one amino acid in the L41 ribosomal protein of yeasts

et al. 1992

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“…In A and B only half of the total amount of protein extracted was applied to the gel. The numbers in C correspond to the nomenclature of Otaka and Osawa [26] concentration was then decreased by dialysing the sample against a solution containing the desired salt concentration. Core particles were sedimented and analysed by exactly the same methods as described above.…”

Section: Effect Qf Licl Treatment On Yeast 60s Ribosomal Subunitsmentioning

confidence: 99%

Stepwise dissociation of yeast 60S ribosomal subunits by LiCl and identification of L25 as a primary 26S rRNA binding protein

El-Baradi

Raué

Regt

et al. 1984

European Journal of Biochemistry

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Treatment of yeast 60s ribosomal subunits with 0.5 M LiCl was found to remove all but six of the ribosomal proteins. The proteins remaining associated with the (26s + 5.8s) rRNA complex were identified as L4, L8, LIO, L12, L16 and L25. These core proteins were split off sequentially in the order (L16 + L12), L10, (L4 + L8), L25by further increasing the LiCl concentration. At 1 .O M LiCl only ribosomal protein L25 remains bound to the rRNA. Upon lowering the LiCl concentration the core proteins reassociate with the rRNA in the reverse order of their removal. The susceptibility of the ribosomal proteins to removal by LiCl corresponds quite well with their order of assembly into the 60s subunit in viva as determined earlier [Kruiswijk et al. (1978) Biochim. Biophys. Acta 517,378 -3891. Binding studies in vitro using partially purified L25 showed that this protein binds specifically to 26s rRNA. Therefore our experiments for the first time directly identify a eukaryotic ribosomal protein capable of binding to high-molecular-mass rRNA. Binding studies in vitro using a blot technique demonstrated that core proteins L8 and L16 as well as protein L21, though not present in any of the core particles, are also capable of binding to 26s rRNA to approximately the same extent as L25. About nine additional 60s proteins appeared to interact with the 26s rRNA, though to a lesser extent.Structural and functional studies on prokaryotic ribosomes have benefited enormously from our ability to take ribosomal subunits apart and reassemble the components again into biologically active particles. A widely used technique for controlled dissociation of ribosomal constituents is treatment of ribosomal subunits with high concentrations of monovalent cations, notably LiC1. Such treatment results in removal of a portion of the ribosomal proteins, leaving discrete core particles on which a well-defined subset of the ribosomal proteins remains [I -31. Such cores have played an important role in establishing structure-function relationships for various prokaryotic ribosomal components (see for instance [4]) and continue to be used for this purpose [5, 61. Moreover, the split protein fractions obtained by LiCl treatment are an excellent source of partially purified ribosomal proteins, the conformation of which appears not to be unduly disturbed by this extraction method [7].

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“…The protein, designated as L23, is acidic and belongs to the 60S subunit (Ishiguro 1984). From the relative mobilities on two-dimensional gels, this protein may correspond to L26 described in the previous report (Ishiguro 1976), to L24 in Kruiswijk and Planta (1974) and to YL31 in Otaka and Osawa (1981). It is of interest that the drastic change in isoelectric point of the protein by mutation did not affect cell growth (doubling time, 100 min) and ability for sporulation.…”

Section: Preparationmentioning

confidence: 74%

Isolation and characterization of a mutant having an altered ribosomal protein in the yeast, Saccharomyces cerevisiae.

Ishiguro

1985

The Japanese journal of genetics

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A cycloheximide-resistant mutant which also displays coreversion of leu2-1 UAA and met8-1 UAG mutations was isolated and characterized in the yeast, S. cerevisiae. One of the ribosomal protein (L23) differed electrophoretically in the mutant strain from that of the parental one. Diploid cells heterozygous for the mutation contained both altered and normal proteins and gave rise to tetrads of 2:2 segregation for the protein alteration, indicating that a single structural gene coding for L23 protein was mutated.In the meiotic progenies, however, alteration of the L23 protein did not cosegregate with any phenotypes of cycloheximide-resistance or reversion of the nonsense mutations.Trisomic analysis was performed to determine the genetic locus for the L23 protein, suggesting that the gene may not be on the chromosomes I through XVI examined.

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Yeast ribosomal proteins: V. Correlation of several nomenclatures and proposal of a standard nomenclature

Cited by 77 publications

References 16 publications

Drastic alteration of cycloheximide sensitivity by substitution of one amino acid in the L41 ribosomal protein of yeasts

Drastic alteration of cycloheximide sensitivity by substitution of one amino acid in the L41 ribosomal protein of yeasts

Stepwise dissociation of yeast 60S ribosomal subunits by LiCl and identification of L25 as a primary 26S rRNA binding protein

Isolation and characterization of a mutant having an altered ribosomal protein in the yeast, Saccharomyces cerevisiae.

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