The sequence of a cDNA encoding ribosomal protein S14 from the hydrozoan Podocoryne carnea reveals high evolutionary conservation

Aerne, Birgit L.; Baader, Christine D.; Schmid, Volker; Schuchert, Peter

doi:10.1016/0378-1119(94)90551-7

Cited by 4 publications

(2 citation statements)

References 15 publications

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“…For example, the amino acid sequences of rp59 protein encoded by the S. cerevisiae CRY1 and CRY2 genes and the rpS14 protein encoded by the mammalian RPS14 gene are 80% identical (31,55). However, the number, size, and location of introns within genes encoding rp59 and its homologs differ radically (2,6,33,51,55,65). The yeast genes contain one intron interrupting codon 3 or 4, whereas the metazoan genes contain multiple introns at different locations (56).…”

Section: Fig 10mentioning

confidence: 99%

Feedback Inhibition of the Yeast Ribosomal Protein Gene CRY2 Is Mediated by the Nucleotide Sequence and Secondary Structure of CRY2 Pre-mRNA

Paulovich

Woolford

1995

Molecular and Cellular Biology

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The Saccharomyces cerevisiae CRY1 and CRY2 genes, which encode ribosomal protein rp59, are expressed at a 10:1 ratio in wild-type cells. Deletion or inactivation of CRY1 leads to 5-to 10-fold-increased levels of CRY2 mRNA. Ribosomal protein 59, expressed from either CRY1 or CRY2, represses expression of CRY2 but not CRY1. cis-Acting elements involved in repression of CRY2 were identified by assaying the expression of CRY2-lacZ gene fusions and promoter fusions in CRY1 CRY2 and cry1-⌬ CRY2 strains. Sequences necessary and sufficient for regulation lie within the transcribed region of CRY2, including the 5 exon and the first 62 nucleotides of the intron. Analysis of CRY2 point mutations corroborates these results and indicates that both the secondary structure and sequence of the regulatory region of CRY2 pre-mRNA are necessary for repression. The regulatory sequence of CRY2 is phylogenetically conserved; a very similar sequence is present in the 5 end of the RP59 gene of the yeast Kluyveromyces lactis. Wild-type cells contain very low levels of both CRY2 pre-mRNA and CRY2 mRNA. Increased levels of CRY2 pre-mRNA are present in mtr mutants, defective in mRNA transport, and in upf1 mutants, defective in degradation of cytoplasmic RNA, suggesting that in wild-type repressed cells, unspliced CRY2 pre-mRNA is degraded in the cytoplasm. Taken together, these results suggest that feedback regulation of CRY2 occurs posttranscriptionally. A model for coupling ribosome assembly and regulation of ribosomal protein gene expression is proposed.The expression of ribosomal genes is coordinately regulated so that equimolar amounts of rRNAs and ribosomal proteins accumulate for assembly into ribosomes. The rate of synthesis of ribosomal molecules is also tightly coordinated with the physiological state of cells (reviewed in references 72 and 73). Coordinate synthesis of yeast ribosomal proteins is controlled primarily at the level of transcription of their genes through one of two common upstream activating sequences, UAS RPG or UAS T (reviewed in references 72 and 73). Posttranscriptional controls provide mechanisms for fine-tuning the expression of individual ribosomal protein (rp) genes (1,7,14,41,50,53,64,69).Balanced accumulation of ribosomal proteins in Escherichia coli results from feedback regulation of their expression (reviewed in references 47 and 48). Certain E. coli ribosomal proteins, when synthesized in excess of the rRNAs to which they bind in the assembling ribosome, repress expression of their own operons. Four eukaryotic rp genes have also been found to be autogenously regulated. Yeast ribosomal protein L32 binds to a structure comprising the 5Ј exon and the first few nucleotides of the intron of RPL32 pre-mRNA and blocks its splicing (15, 67). L32 also regulates the translation of its own mRNA through a similar secondary structure formed in the 5Ј end of the mature mRNA (8). Expression of the yeast rp gene RPL2 is autogenously controlled at the level of mRNA accumulation (53). The Xenopus laevis gene that encod...

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Section: Fig 10mentioning

confidence: 99%

Feedback Inhibition of the Yeast Ribosomal Protein Gene CRY2 Is Mediated by the Nucleotide Sequence and Secondary Structure of CRY2 Pre-mRNA

Paulovich

Woolford

1995

Molecular and Cellular Biology

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“…Chemically-induced mutations near the 3′-end of RPS14 in Chinese hamster ovary CHO-K1 cells are responsible for recessive resistance to the translational inhibitor emetine; and CHO-K1 cells expressing this phenotype can be isolated efficiently in tissue culture (Gupta and Siminovitch, 1977;Boersma et al, 1979a,b;Madjar et al, 1983;Tasheva and Roufa, 1993). Several wild-type and mutant RPS14 alleles have been obtained as cloned cDNAs (Rhoads and Roufa, 1985;Chen et al, 1986;Nakamichi et al, 1986) and chromosomal segments (Rhoads et al, 1986;Rhoads and Roufa, 1991) from Chinese hamster and human cells as well as from a variety of other eukaryotic species (Larkin et al, 1987;Brown et al, 1988;Larkin et al, 1989;Paz et al, 1989;Perelman and Boothroyd, 1990;Tyler and Harrison, 1990;Larson and Rossi, 1991;Aerne et al, 1994;Nelson et al, 1994;Wilson et al, 1994). Further, CHO cell lines carrying transgenic S14 DNA sequences have been constructed to characterize the biological activities of mutationally altered RPS14 genes (Diaz et al, 1990(Diaz et al, , 1991Diaz and Roufa, 1992;Roufa, 1996).…”

Section: Introductionmentioning

confidence: 99%

Functional analysis of human RPS14 null alleles

Martı́n-Nieto

Roufa

1997

Journal of Cell Science

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Previously we described a large collection of cloned human DNAs that encode chemically defined missense mutations within the ribosomal protein S14 sequence. We determined that biologically inactive (i.e. null) alleles resulted primarily from point mutations targeted to two internal segments of the S14-coding sequence and designated these functionally critical regions as domains B and D. Further, we inferred that structural determinants within domains B and D are required for proper incorporation of the S14 protein into nascent 40 S ribosomal particles and/or for the normal function of mature cytoplasmic ribosomes. In this study we have used immunofluorescence to monitor the intracellular trafficking of epitopically labeled human S14 protein isoforms transiently expressed by cultured Chinese hamster cells. Data obtained distinguish null alleles of RPS14 which encode proteins that are not incorporated into pre-ribosomal subunit particles from null alleles whose products are compatible with normal ribosome assembly processes but result in functionally inactive cytoplasmic 40 S ribosomal subunits. Mutations assigned to the first allele class involve amino acid replacements located within S14 domains B and D; whereas mutations assigned to the second class are distributed throughout the S14 protein-coding sequence.

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Nucleotide sequence of ub52 from the cnidarian Acropora millepora reveals high evolutionary conservation

Berghammer

Hayward

Harrison

et al. 1996

Gene

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The sequence of a cDNA encoding ribosomal protein S14 from the hydrozoan Podocoryne carnea reveals high evolutionary conservation

Cited by 4 publications

References 15 publications

Feedback Inhibition of the Yeast Ribosomal Protein Gene CRY2 Is Mediated by the Nucleotide Sequence and Secondary Structure of CRY2 Pre-mRNA

Feedback Inhibition of the Yeast Ribosomal Protein Gene CRY2 Is Mediated by the Nucleotide Sequence and Secondary Structure of CRY2 Pre-mRNA

Functional analysis of human RPS14 null alleles

Nucleotide sequence of ub52 from the cnidarian Acropora millepora reveals high evolutionary conservation

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