Synthesis and turnover of ribosomal proteins in the absence of 60S subunit assembly in Saccharomyces cerevisiae

Gorenstein, Charles; Warner, Jonathan R.

doi:10.1007/bf00268670

Cited by 77 publications

(52 citation statements)

References 21 publications

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“…In a 3-min pulse, the unassembled half-life of these proteins would have to be less than 1 min if turnover alone were responsible for the observed labeling. The half-life of 60S ribosomal proteins synthesized in the absence of rRNA was measured previously at 7 to 20 min (11). In that experiment proteins L2, L5, and L13 (designated rp2, rp8, and rpl5 in reference 11) had half-lives of 24, 8, and 13 min, respectively.…”

Section: Methodsmentioning

confidence: 96%

Effects of progressive depletion of TCM1 or CYH2 mRNA on Saccharomyces cerevisiae ribosomal protein accumulation.

Nam¹,

Fried

1986

Mol. Cell. Biol.

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When present in excess, the mRNAs for Saccharomyces cerevisiae ribosomal proteins L3 and L29 are translated less efficiently, so that synthesis of these proteins remains commensurate with that of other ribosomal proteins (N. J. Pearson, H. M. Fried, and J. R. Warner, CeUl 29:347-355, 1982; J. R. Warner, G. Mitra, W. F. Schwindinger, M. Studeny, and H. M. Fried, Mol. Cell. Biol. 5:1512-1521. We used a yeast strain with a conditionally transcribed derivative of the L3 gene to deplete cells progressively of L3 mRNA. In this case translation of L3 mRNA did not become more efficient so that L3 was not maintained at a normal level. Even when there was an initial excess of L3 mRNA, interruption of its further transcription produced an immediate drop in L3 synthesis, suggesting that the translational efficiency of preexisting mRNA cannot be altered. Lack of L3 synthesis afforded an opportunity to examine coordinate accumulation of other ribosomal proteins. Without L3, apparent synthesis of several 60S subunit proteins diminished, and 60S subunits did not assemble. A similar phenomenon occurred when, in a second strain, synthesis of ribosomal protein L29 was prevented. Loss of 60S subunit assembly was accompanied by a destabilization of some 60S ribosomal protein mRNAs. These data suggest that synthesis of some S. cerevisiae ribosomal proteins may be regulated posttranscriptionally as a function of the extent to which they are assembled.Saccharomyces cerevisiae strains growing in stable environmental circumstances accumulate each of 70 or so ribosomal proteins in a stoichiometric and coordinate fashion. This situation exists in part because most proteins appear to be present in a single copy in the ribosome and because unassembled ribosomal proteins account for little if any of the total amount of ribosomal protein (see reference 27 for a review). Besides providing a sufficient number of ribosomes for a given growth condition, the rigorous coordination of ribosomal protein accumulation prevents the waste of synthetic energy, which may be especially important as these proteins are among the more abundant in most cells. In S. cerevisiae, an example of non-overproduction of a ribosomal protein was found by increasing the gene number for ribosomal protein L3; despite an elevated amount of L3 mRNA, no increased synthesis of L3 was observed (23) While yeast cells appear to reduce translation of some ribosomal protein mRNAs when present in excess, it is not known how this regulation comes about, although for L3 and L29 it is known that the excess mRNA is actually in polyribosomes and is thus translated (28). For L3, an overabundance of its mRNA causes that transcript to appear in smaller polyribosomes, suggesting that translational initiation is reduced. The agent which brings about reduced translation is unknown, but by analogy with ribosome regulation in Escherichia coli (21) may be connected to the presence of more protein than can be assembled.Previously we reported that S. cerevisiae strains with a partially inactivated pr...

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Section: Methodsmentioning

confidence: 96%

Effects of progressive depletion of TCM1 or CYH2 mRNA on Saccharomyces cerevisiae ribosomal protein accumulation.

Nam¹,

Fried

1986

Mol. Cell. Biol.

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“…Previously it was shown that the temperature-sensitive mutant rrp1-1 is defective in the processing of 27S pre-rRNA to produce 25S rRNA and deficient in 32 P -labeled 60S ribosomal subunits (Andrew et al 1976;Gorenstein and Warner 1977;Fabian and Hopper 1987). We sought to examine the function of Rrp1p in more detail by constructing and assaying a mutant strain containing a conditional null allele of RRP1, and by assaying pre-rRNA processing at higher resolution in rrp1 mutants.…”

Section: Depletion or Inactivation Of Rrp1p Leads To Defects In Biogementioning

confidence: 99%

“…Although it was shown that processing of 27S pre-rRNA to mature 25S and 5.8S rRNAs was blocked in the rrp1-1 mutant, tools were not yet available to identify and distinguish the 27SA 2 , 27SA 3 , 27SB S , 27SB L , and 25.5S pre-rRNA processing intermediates (Andrew et al 1976;Gorenstein and Warner 1977;Fabian and Hopper 1987). Thus, the exact nature of the 27S pre-rRNA processing defect in the rrp1-1 mutant was not clear.…”

Section: Rrp1p Is Important For Two Steps In Pre-rrna Processingmentioning

confidence: 99%

“…The mutation was shown to cause an undefined defect in conversion of 27S pre-rRNA to mature 5.8S and 25S rRNAs, resulting in decreased levels of 60S ribosomal subunits (Andrew et al 1976;Fabian and Hopper 1987;Gorenstein and Warner 1977). Consistent with this mutant phenotype, affinity purifications using several TAP-tagged nucleolar proteins led to the isolation of 66S pre-ribosomes containing 27S pre-rRNAs and a large set of nonribosomal proteins that included Rrp1p (Harnpicharnchai et al 2001;Fatica et al 2002;Gavin et al 2002;Nissan et al 2002;Saveanu et al 2001).…”

Section: Introductionmentioning

confidence: 97%

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Role of the yeast Rrp1 protein in the dynamics of pre-ribosome maturation

Horsey

Jakovljevic²,

Miles³

et al. 2004

RNA

109

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The Saccharomyces cerevisiae gene RRP1 encodes an essential, evolutionarily conserved protein necessary for biogenesis of 60S ribosomal subunits. Processing of 27S pre-ribosomal RNA to mature 25S rRNA is blocked and 60S subunits are deficient in the temperature-sensitive rrp1-1 mutant. We have used recent advances in proteomic analysis to examine in more detail the function of Rrp1p in ribosome biogenesis. We show that Rrp1p is a nucleolar protein associated with several distinct 66S pre-ribosomal particles. These pre-ribosomes contain ribosomal proteins plus at least 28 nonribosomal proteins necessary for production of 60S ribosomal subunits. Inactivation of Rrp1p inhibits processing of 27SA 3 to 27SB S pre-rRNA and of 27SB pre-rRNA to 7S plus 25.5S pre-rRNA. Thus, in the rrp1-1 mutant, 66S pre-ribosomal particles accumulate that contain 27SA 3 and 27SB L pre-ribosomal RNAs.

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“…The coordination did not, however, appear to be at the level of synthesis. Indeed, in most cases, inhibited synthesis of one component did not effect the synthesis of the other [12,13,16]. The reduced accumulation of the latter was due to increased degradation.…”

Section: Discussionmentioning

confidence: 95%

The synthesis of ribosomal RNA and ribosomal protein and their incorporation into ribosomes in the uterus of the oestrogen‐stimulated immature rat

Müller

Knowler

1984

FEBS Letters

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The effect of oestrogen on the synthesis of ribosomal proteins in the uterus of the immature rat has been investigated. Stimula~ synthesis peaks, at 6-7-times control levels, 12 h after a single administration of the hormone, The stimulated synthesis and incorporation of newly made proteins into ribosomal particles exhibit very similar kinetics. The incorporation of newly made rRNA into ribosomes mirrors that of ribosomai protein but lags several hours behind the peak of oestrogen-stimulated rRNA synthesis.Cell-free protein synthesis Immunoassuy

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Synthesis and turnover of ribosomal proteins in the absence of 60S subunit assembly in Saccharomyces cerevisiae

Cited by 77 publications

References 21 publications

Effects of progressive depletion of TCM1 or CYH2 mRNA on Saccharomyces cerevisiae ribosomal protein accumulation.

Effects of progressive depletion of TCM1 or CYH2 mRNA on Saccharomyces cerevisiae ribosomal protein accumulation.

Role of the yeast Rrp1 protein in the dynamics of pre-ribosome maturation

The synthesis of ribosomal RNA and ribosomal protein and their incorporation into ribosomes in the uterus of the oestrogen‐stimulated immature rat

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