Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae

Espinar-Marchena, Francisco J.; Rodríguez-Galán, Olga; Fernández-Fernández, José; Linnemann, Jan; Cruz, Jesús de la

doi:10.1093/nar/gky123

Cited by 17 publications

(10 citation statements)

References 141 publications

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“…This fact is likely due to the weak and/or transient association of Pol5 with preribosomal particles. Indeed, the enrichment of 27S pre-rRNAs we obtained by the affinity purification of GFP-tagged Pol5 was clearly poorer than what we have previously observed for purifications of other GFPtagged ribosome biogenesis factors or r-proteins (e.g., Babiano and de la Cruz 2010;Espinar-Marchena et al 2018).…”

Section: Discussioncontrasting

confidence: 82%

Pol5 is an essential ribosome biogenesis factor required for 60S ribosomal subunit maturation in Saccharomyces cerevisiae

Ramos-Sáenz

González-Álvarez

Rodríguez-Galán

et al. 2019

RNA

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In Saccharomyces cerevisiae, more than 250 trans-acting factors are involved in the maturation of 40S and 60S ribosomal subunits. The expression of most of these factors is transcriptionally coregulated to ensure correct ribosome production under a wide variety of environmental and intracellular conditions. Here, we identified the essential nucleolar Pol5 protein as a novel trans-acting factor required for the synthesis of 60S ribosomal subunits. Pol5 weakly and/or transiently associates with early to medium pre-60S ribosomal particles. Depletion of and temperature-sensitive mutations in Pol5 result in a deficiency of 60S ribosomal subunits and accumulation of half-mer polysomes. Both processing of 27SB pre-rRNA to mature 25S rRNA and release of pre-60S ribosomal particles from the nucle(ol)us to the cytoplasm are impaired in the Pol5depleted strain. Moreover, we identified the genes encoding ribosomal proteins uL23 and eL27A as multicopy suppressors of the slow growth of a temperature-sensitive pol5 mutant. These results suggest that Pol5 could function in ensuring the correct folding of 25S rRNA domain III; thus, favoring the correct assembly of these two ribosomal proteins at their respective binding sites into medium pre-60S ribosomal particles. Pol5 is homologous to the human tumor suppressor Myb-binding protein 1A (MYBBP1A). However, expression of MYBBP1A failed to complement the lethal phenotype of a pol5 null mutant strain though interfered with 60S ribosomal subunit biogenesis.

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Section: Discussioncontrasting

confidence: 82%

Pol5 is an essential ribosome biogenesis factor required for 60S ribosomal subunit maturation in Saccharomyces cerevisiae

Ramos-Sáenz

González-Álvarez

Rodríguez-Galán

et al. 2019

RNA

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“…Another important cytoplasmic protein—ribosomal protein L14 in E. coli binds directly to 23S ribosomal RNA and forms part of bridges connecting the 2 ribosomal subunits. When L14 protein interacts with RsfS, the bridge cannot be formed, and the 30S and 50S ribosomal subunits do not associate, which represses translation 29 . ATP-dependent and ATP-binding subunit HslU proteases are enzymes which operate by a variety of chemical mechanisms and are essential for bacterial cell life and pathogenicity.…”

Section: Discussionmentioning

confidence: 99%

Amikacin and bacteriophage treatment modulates outer membrane proteins composition in Proteus mirabilis biofilm

Maszewska

Moryl

et al. 2021

Sci Rep

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Modification of outer membrane proteins (OMPs) is the first line of Gram-negative bacteria defence against antimicrobials. Here we point to Proteus mirabilis OMPs and their role in antibiotic and phage resistance. Protein profiles of amikacin (AMKrsv), phage (Brsv) and amikacin/phage (AMK/Brsv) resistant variants of P. mirabilis were compared to that obtained for a wild strain. In resistant variants there were identified 14, 1, 5 overexpressed and 13, 5, 1 downregulated proteins for AMKrsv, Brsv and AMK/Brsv, respectively. Application of phages with amikacin led to reducing the number of up- and downregulated proteins compared to single antibiotic treatment. Proteins isolated in AMKrsv are involved in protein biosynthesis, transcription and signal transduction, which correspond to well-known mechanisms of bacteria resistance to aminoglycosides. In isolated OMPs several cytoplasmic proteins, important in antibiotic resistance, were identified, probably as a result of environmental stress, e.g. elongation factor Tu, asparaginyl-tRNA and aspartyl-tRNA synthetases. In Brsv there were identified: NusA and dynamin superfamily protein which could play a role in bacteriophage resistance. In the resistant variants proteins associated with resistance mechanisms occurring in biofilm, e.g. polyphosphate kinase, flagella basal body rod protein were detected. These results indicate proteins important in the development of P. mirabilis antibiofilm therapies.

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“…It is known that many ribosomal proteins play important roles in ribosome biogenesis and mutations introduced in these proteins often result in accumulation of unprocessed immature ribosomes (Biedka et al, 2018;Espinar-Marchena et al, 2018;Tomioka et al, 2018;Cheng et al, 2019). Previous studies have also shown that specific mutations/deletions of RACK1 or uS3 impact ribosome biogenesis (Larburu et al, 2016;Mitterer et al, 2016;Limoncelli et al, 2017).…”

Section: Disruption Of Rack1 Binding To the Ribosome Perturbs Global mentioning

confidence: 99%

Communication between RACK1/Asc1 and uS3 (Rps3) is essential for RACK1/Asc1 function in yeast Saccharomyces cerevisiae

Singh

Jindal

Ghosh

et al. 2019

Gene

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The receptor for activated c-kinase (RACK1, Asc1 in yeast) is a eukaryotic ribosomal protein located in the head region of the 40S subunit near the mRNA exit channel. This WD-repeat βpropeller protein acts as a signaling molecule and is involved in metabolic regulation, cell cycle progression, and translational control. However, the exact details of the RACK1 recruitment and stable association with the 40S ribosomal subunit remain only partially known. X-ray analyses of the yeast, Saccharomyces cerevisiae, ribosome revealed that the RACK1 propeller blade (4-5) interacts with the eukaryote-specific C-terminal domain (CTD) of ribosomal protein S3 (uS3 family). To check the functional significance of this interaction, we generated mutant yeast strains harboring C-terminal deletions of uS3. We found that deletion of the 20 C-terminal residues (interacting with blade 4-5) from the uS3-CTD abrogates RACK1 binding to the ribosome. Strains with truncated uS3-CTD exhibited compromised cellular growth and protein synthesis similar to that of RACK1Δ strain, thus suggesting that the uS3-CTD is crucial not only for the recruitment and association of RACK1 with the ribosome, but also for its intracellular function. We suggest that eukaryote-specific RACK1-uS3 interaction has evolved to act as a link between the ribosome and the cellular signaling pathways.

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Ribosomal protein L14 contributes to the early assembly of 60S ribosomal subunits in Saccharomyces cerevisiae

Cited by 17 publications

References 141 publications

Pol5 is an essential ribosome biogenesis factor required for 60S ribosomal subunit maturation in Saccharomyces cerevisiae

Pol5 is an essential ribosome biogenesis factor required for 60S ribosomal subunit maturation in Saccharomyces cerevisiae

Amikacin and bacteriophage treatment modulates outer membrane proteins composition in Proteus mirabilis biofilm

Communication between RACK1/Asc1 and uS3 (Rps3) is essential for RACK1/Asc1 function in yeast Saccharomyces cerevisiae

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