Autoregulation in the Biosynthesis of Ribosomes

Zhao, Yu; Sohn, Jung‐Hoon; Warner, Jonathan R.

doi:10.1128/mcb.23.2.699-707.2003

Cited by 76 publications

(75 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It may be a general phenomenon that when the level of any nucleolar protein related to mammalian rRNA production falls below or raises above a threshold value, the architecture of preribosome processing machineries collapses, sending feedback regulatory signals to RNA polymerase I or rRNA-degrading complexes. It is known that the tightly regulated rRNA production depends on several cellular signals (9,46). This might explain why down-regulation of RH-II/Gu␣ (this study) or dyskerin (17) or up-regulation of p19 arf (15) results in similar inhibitory effects on rRNA production.…”

Section: Fig 6 Overexpression Of Rh-ii/gu␤ Blocks Rrna Productionmentioning

confidence: 52%

Silencing of RNA Helicase II/Guα Inhibits Mammalian Ribosomal RNA Production

Henning

Jin

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Section: Fig 6 Overexpression Of Rh-ii/gu␤ Blocks Rrna Productionmentioning

confidence: 52%

Silencing of RNA Helicase II/Guα Inhibits Mammalian Ribosomal RNA Production

Henning

Jin

et al. 2003

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…In the absence of Yvh1, mutant Pma1-10 turnover from the plasma membrane is prevented, permitting cell growth ( Figure 1 . Analogously, a requirement for 60S assembly in regulating events at the plasma membrane has previously been reported (Miyoshi et al 2002;Zhao et al 2003). Even so, it is a challenge to reconcile involvement of Yvh1 in ribosome assembly and its role in turnover of mutant Pma1-10 from the cell surface.…”

Section: Discussionmentioning

confidence: 97%

“…Also, we cannot exclude the possibility that the pma1-10 suppressors may act by reducing 60S subunits. In this regard, it is of interest that repression of ribosome synthesis in response to a defect in the secretory pathway is suppressed by a deficiency in 60S ribosomal subunits (although the mechanism by which this occurs is not known) (Zhao et al 2003).…”

Section: Discussionmentioning

confidence: 99%

A Mutant Plasma Membrane Protein Is Stabilized Upon Loss of Yvh1, a Novel Ribosome Assembly Factor

Liu

Chang

2009

Genetics

View full text Add to dashboard Cite

Pma1-10 is a mutant plasma membrane ATPase defective at the restrictive temperature in stability at the cell surface. At 37°, Pma1-10 is ubiquitinated and internalized from the plasma membrane for degradation in the vacuole. YVH1, encoding a tyrosine phosphatase, is a mutant suppressor of pma1-10 ; in the absence of Yvh1, Pma1-10 remains stable at the plasma membrane, thereby permitting cells to grow. The RING finger domain of Yvh1, but not its phosphatase domain, is required for removal of mutant Pma1-10 from the plasma membrane. Yvh1 is a novel ribosome assembly factor: in yvh1D cells, free 60S and 80S ribosomal subunits are decreased, free 40S subunits are increased, and half-mer polysomes are accumulated. Pma1-10 is also stabilized by deletion of 60S ribosomal proteins Rpl19a and Rpl35a. We propose that changes in ribosome biogenesis caused by loss of Yvh1 or specific ribosomal proteins have effects on the plasma membrane, perhaps by producing specific translational changes.

show abstract

“…Interestingly, deletion of some RPGs has been shown to alter the transcriptional response to tunicamycin (Zhao et al 2003). Hac1-independent resistance in rpDs could also be a result of enhanced translation of chaperones or other factors that aid in folding in the ER, as deletion of particular RPGs is known to result in enhanced translation of at least one specific message, GCN4 (Foiani et al 1991;MartinMarcos et al 2007;Steffen et al 2008), and the generality of this phenomenon has not been globally assessed.…”

Section: Rps Tunicamycin Resistance and Life Spanmentioning

confidence: 99%

Ribosome Deficiency Protects Against ER Stress in Saccharomyces cerevisiae

et al. 2012

View full text Add to dashboard Cite

In Saccharomyces cerevisiae, 59 of the 78 ribosomal proteins are encoded by duplicated genes that, in most cases, encode identical or very similar protein products. However, different sets of ribosomal protein genes have been identified in screens for various phenotypes, including life span, budding pattern, and drug sensitivities. Due to potential suppressors of growth rate defects among this set of strains in the ORF deletion collection, we regenerated the entire set of haploid ribosomal protein gene deletion strains in a clean genetic background. The new strains were used to create double deletions lacking both paralogs, allowing us to define a set of 14 nonessential ribosomal proteins. Replicative life-span analysis of new strains corresponding to ORF deletion collection strains that likely carried suppressors of growth defects identified 11 new yeast replicative aging genes. Treatment of the collection of ribosomal protein gene deletion strains with tunicamycin revealed a significant correlation between slow growth and resistance to ER stress that was recapitulated by reducing translation of wild-type yeast with cycloheximide. Interestingly, enhanced tunicamycin resistance in ribosomal protein gene deletion mutants was independent of the unfolded protein response transcription factor Hac1. These data support a model in which reduced translation is protective against ER stress by a mechanism distinct from the canonical ER stress response pathway and further add to the diverse yet specific phenotypes associated with ribosomal protein gene deletions.T HE yeast ribosome consists of two subunits, the 40S (small) and 60S (large), which together contain four discrete rRNA species and 78 ribosomal proteins (RPs). In Saccharomyces cerevisiae, 59 of the 78 ribosomal proteins are encoded by a pair of paralogous genes, most of which arose through a genome-wide duplication event roughly 100 million years ago (Wolfe and Shields 1997). Only 12% of the duplicated genome remains, and of the paralogous gene pairs present, a majority of ribosomal proteins genes (RPGs) are in a class that exhibits little or even decelerated evolution (Kellis et al. 2004). Remarkably, 21 of the 59 RPG pairs encode identical proteins, and the others are highly similar (Supporting Information, Table S1). The prevalence of synthetic lethality among RPG paralogs indicates that the two protein products are generally redundant for at least one essential function (Dean et al. 2008).Despite the significant similarity among RPG paralogs, many reports have described differential effects of deleting only one, and such instances have been observed even in cases where the encoded protein product is identical (Briones et al. 1998). One explanation for this is that the two genes contribute different amounts of protein, and neither is alone sufficient to support wild-type growth. In the case of Rpl16, for example, expression of either RPL16A or RPL16B can rescue the growth defect of cells lacking RPL16B (Rotenberg et al. 1988). Consistently, the RPL16...

show abstract

Autoregulation in the Biosynthesis of Ribosomes

Cited by 76 publications

References 40 publications

Silencing of RNA Helicase II/Guα Inhibits Mammalian Ribosomal RNA Production

Silencing of RNA Helicase II/Guα Inhibits Mammalian Ribosomal RNA Production

A Mutant Plasma Membrane Protein Is Stabilized Upon Loss of Yvh1, a Novel Ribosome Assembly Factor

Ribosome Deficiency Protects Against ER Stress in Saccharomyces cerevisiae

Contact Info

Product

Resources

About