Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae.

Remacha, Miguel; Sáenz-Robles, Maria Teresa; Vilella, Maria Dolores; Ballesta, Juan P. G.

doi:10.1016/s0021-9258(19)76513-2

Cited by 95 publications

(25 citation statements)

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“…Transcription of the four RPA genes therefore appears to be controlled independently. DISCUSSION It had been shown previously that multicellular organisms (a crustacean, an insect, and a vertebrate) contain two small acidic ribosomal proteins (15,25,28,42), whereas the budding yeast S. cerevisiae contains four distinct proteins (19,20,26). We report here that the distantly related yeast S. pombe contains four genes for small A-type ribosomal proteins, confirming the suggestion that this might be a characteristic of lower eucaryotes (26).…”

Section: Ttgagcctatctgggcaaccatctttgctaaggctttggagggcaaggacttgaaggaactccttttgaacattggctctgctgctgccgctcctgctgc E P I W a T I Fsupporting

confidence: 89%

“…The sequences of the cDNAs demonstrate that the multicellular organisms contain two genes, coding for proteins that have been extremely conserved during evolution. S. cerevisiae, on the other hand, contains four independent genes for small acidic ribosomal proteins, which have been called Al (19), L44' (26), L45 (26), and L44 (26), alternatively named A2 (20). Proteins L44 and L45 are very similar to each other, as are proteins Al and L44', suggesting that each of the A-proteins of higher organisms has two counterparts in yeast cells.…”

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confidence: 99%

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A Gene Family for Acidic Ribosomal Proteins in Schizosaccharomyces pombe: Two Essential and Two Nonessential Genes

Beltrame

Bianchi

1990

Molecular and Cellular Biology

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We have cloned the genes for small acidic ribosomal proteins (A-proteins) of the fission yeast Schizosaccharomyces pombe. S. pombe contains four transcribed genes for small A-proteins per haploid genome, as is the case for Saccharomyces cerevisiae. In contrast, multicellular eucaryotes contain two transcribed genes per haploid genome. The four proteins of S. pombe, besides sharing a high overall similarity, form two couples of nearly identical sequences. Their corresponding genes have a very conserved structure and are transcribed to a similar level. Surprisingly, of each couple of genes coding for nearly identical proteins, one is essential for cell growth, whereas the other is not. We suggest that the unequal importance of the four small A-proteins for cell survival is related to their physical organization in 60S ribosomal subunits.

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Section: Ttgagcctatctgggcaaccatctttgctaaggctttggagggcaaggacttgaaggaactccttttgaacattggctctgctgctgccgctcctgctgc E P I W a T I Fsupporting

confidence: 89%

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confidence: 99%

A Gene Family for Acidic Ribosomal Proteins in Schizosaccharomyces pombe: Two Essential and Two Nonessential Genes

Beltrame

Bianchi

1990

Molecular and Cellular Biology

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“…The plasmids were constructed by subcloning either the wild-type (pFL36-L44) or different mutated rpYP2R genes (pFL36-L44cys71, pFL36-L44cys79, pFL36-L44cys71/79) from BS-L44 in the BamHI-SmaI sites of the centromeric vector pFL36 (Bonneaud et al, 1991). BS-L44 was obtained by cloning in the EcoRI site of Bluescript KS, a 2.3 kbp EcoRI-EcoRI fragment from plasmid pMRE44 (Remacha et al, 1988) containing the wildtype rpYP2R gene. Site-directed mutagenesis was carried out by PCR (Dieffenbach & Dveksler, 1995) on plasmid BS-L44 using mutagenic oligonucleotides prepared by Isogen Bioscience (Maarsen, The Netherlands).…”

Section: Plasmidsmentioning

confidence: 99%

Phosphorylation of the Acidic Ribosomal P Proteins in Saccharomyces cerevisiae: A Reappraisal

et al. 1997

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Previous reports had pointed to serines 62 and 71/79 as possible phosphorylation sites in the yeast acidic ribosomal proteins YP1 alpha and YP2 alpha, respectively. However, it has been found that mutation of these serine residues did not affect the phosphorylation level of the proteins. A detailed examination of the YP2 alpha tryptic digest from the in vivo labeled protein demonstrates the existence of a totally trypsin-insensitive site at lysine 88 that led to a misinterpretation of previous results. The unique YP2 alpha tryptic phosphopeptide obtained contains, in addition to serines 71 and 79, a serine at position 96 near the carboxyl end, which automatic Edman degradation confirmed as the phosphorylated residue. In addition, by using Staphyloccocus protease V8, it was possible to obtain phosphopeptides containing only serine 96, whose phosphorylation has likewise been confirmed by radioactive labeling as well as by chemical methods. A similar analysis of the other 12 kDa acidic proteins, YP1 alpha, YP1 beta, and YP2 beta, has shown the presence of equivalent phosphorylation sites in the four P proteins, which correspond to position 96 in proteins YP1 alpha, YP1 beta, and YP2 alpha and position 100 in YP2 beta. This conclusion has been confirmed by the fact that mutation of serine 96 in proteins YP1 alpha and YP2 alpha abolishes their capacity to be phosphorylated in vivo. The mutation of the phosphorylation site of the individual acidic proteins seems not to alter their interaction with the ribosome. However, it has been found that the level of phosphorylation of the stalk proteins has an effect on the response of the cells to some specific metabolic conditions, indicating that it may modulate the translation of specific proteins.

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“…Eukaryotic P proteins differ from eubacterial L7/L12 in four main aspects. First, they are encoded by independent genes (Maassen et al, 1985;Rich & Steitz, 1987; Mitsui & Tsurugi, 1988a,b;Remacha et al, 1988;Beltrame & Bianchi, 1990; Newton et al, 1990;Wool et al, 1991). Second, they are phosphorylated on ribosomes (Zinker & Warner, 1976;Juan-Vidales et al, 1984;Naranda & Ballesta, 1991;Naranda et al, 1993), which is why they were named P proteins (Tsurugi et al, 1978), and dephosphorylated in a cytoplasmic pool (van Agthoven et al, 1978;Zinker, 1980;Mitsui et al, 1988).…”

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confidence: 99%

“…The acidic protein genes from human cells (Rich & Steitz, 1987), rat liver (Wool et al, 1991), Anemia salina (Maassen 0006-2960/95/0434-7941 $09.00/0 © 1995 American Chemical Society et al, 1985) Drosophila melanogaster (Qian et al, 1987), Schysosaccharomyces pombe (Beltrame & Bianchi, 1990) and S. cerevisiae (Mitsui & Tsurugi, 1988a,b;Remacha et al, 1988;Newton et al, 1990) have been cloned. Their primary DNA sequences demonstrate that the encoded proteins are of two similar classes, PI and P2, that have been extremely conserved during evolution (Shimmin et al, 1989).…”

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confidence: 99%

Eukaryotic acidic phosphoproteins interact with the ribosome through their amino-terminal domain

Jose

Santana-Roman²,

Remacha³

et al. 1995

Biochemistry

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Variable-size fragments of the four yeast acidic ribosomal protein genes rpYP1 alpha, rpYP1 beta, rpYP2 alpha and rpYP2 beta were fused to the LacZ gene in the vector series YEp356-358. The constructs were used to transform wild-type Saccharomyces cerevisiae and several gene-disrupted strains lacking different acidic ribosomal protein genes. The distribution of the chimeric proteins between the cytoplasm and the ribosomes, tested as beta-galactosidase activity, was estimated. Hybrid proteins containing around a minimum of 65-75 amino acids from their amino-terminal domain are able to bind to the ribosomes in the presence of the complete native proteins. Hybrid proteins containing no more than 36 amino terminal amino acids bind to the ribosomes in the absence of a competing native protein. The fused YP1-beta-galactosidase proteins are also able to form a complex with the native YP2 type proteins, promoting their binding to the ribosome. The stability of the hybrid polypeptides seems to be inversely proportional to the size of their P protein fragment. These results indicate that only the amino-terminal domain of the eukaryotic P proteins is needed for the P1-P2 complex formation required for interaction with the ribosome. The highly conserved P protein carboxyl end is not implicated in the binding to the particles and is exposed to the medium.

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Independent genes coding for three acidic proteins of the large ribosomal subunit from Saccharomyces cerevisiae.

Cited by 95 publications

References 49 publications

A Gene Family for Acidic Ribosomal Proteins in Schizosaccharomyces pombe: Two Essential and Two Nonessential Genes

A Gene Family for Acidic Ribosomal Proteins in Schizosaccharomyces pombe: Two Essential and Two Nonessential Genes

Phosphorylation of the Acidic Ribosomal P Proteins in Saccharomyces cerevisiae: A Reappraisal

Eukaryotic acidic phosphoproteins interact with the ribosome through their amino-terminal domain

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