Assembly and structure of the SSU processome — a nucleolar precursor of the small ribosomal subunit

Barandun, Jonas; Hunziker, Mirjam; Klinge, Sebastian

doi:10.1016/j.sbi.2018.01.008

Cited by 71 publications

(71 citation statements)

References 50 publications

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“…In yeast, assembly of the small ribosomal subunit starts in the nucleolus, within large complexes called 90S particles or SSU processome [8]. Endonucleolytic cleavages of pre-rRNA release so-called pre-40S particles, which are composed of almost all RPS [9] and the 20S pre-rRNA, a precursor to the 18S rRNA bearing a 200-long nucleotide extension at its 3 end.…”

Section: Introductionmentioning

confidence: 99%

Good Vibrations: Structural Remodeling of Maturing Yeast Pre-40S Ribosomal Particles Followed by Cryo-Electron Microscopy

et al. 2020

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Assembly of eukaryotic ribosomal subunits is a very complex and sequential process that starts in the nucleolus and finishes in the cytoplasm with the formation of functional ribosomes. Over the past few years, characterization of the many molecular events underlying eukaryotic ribosome biogenesis has been drastically improved by the “resolution revolution” of cryo-electron microscopy (cryo-EM). However, if very early maturation events have been well characterized for both yeast ribosomal subunits, little is known regarding the final maturation steps occurring to the small (40S) ribosomal subunit. To try to bridge this gap, we have used proteomics together with cryo-EM and single particle analysis to characterize yeast pre-40S particles containing the ribosome biogenesis factor Tsr1. Our analyses lead us to refine the timing of the early pre-40S particle maturation steps. Furthermore, we suggest that after an early and structurally stable stage, the beak and platform domains of pre-40S particles enter a “vibrating” or “wriggling” stage, that might be involved in the final maturation of 18S rRNA as well as the fitting of late ribosomal proteins into their mature position.

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Section: Introductionmentioning

confidence: 99%

Good Vibrations: Structural Remodeling of Maturing Yeast Pre-40S Ribosomal Particles Followed by Cryo-Electron Microscopy

et al. 2020

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“…More recently, progress in cryo-electron microscopy (cryo-EM) has revealed the structure at a near-atomic resolution of some of these affinity-purified preribosomal particles, including the precise localization of the trans-acting factors that are stably associated with them (for reviews, see Bassler and Hurt 2019;Klinge and Woolford 2019). More importantly, the structures of different particles along the r-subunit assembly pathway provide insights into how trans-acting factors, pre-rRNAs, and r-proteins mechanistically participate during the rearrangements and remodeling events of preribosomal particles throughout their subsequent maturation steps (for reviews, see Konikkat and Woolford 2017;Kressler et al 2017;Peña et al 2017;Barandun et al 2018;Bassler and Hurt 2019;Klinge and Woolford 2019).…”

Section: Introductionmentioning

confidence: 99%

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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“…Ribosome biogenesis is one of the most complex pathway existing in eukaryotic cells. This is due to the high number of factors involved and to the variety of the enzymatic reactions occurring along the entire pathway [1]. In addition, the pathway is physically segregated between the nucleus and the cytoplasm by the nuclear membrane, which acts as a natural checkpoint.…”

Section: Introductionmentioning

confidence: 99%

Domain definition and interaction mapping for the endonuclease complex hNob1/hPno1

2018

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Ribosome biogenesis requires a variety of trans-acting factors in order to produce functional ribosomal subunits. In human cells, the complex formed by the proteins hNob1 and hPno1 is crucial to the site 3 cleavage occurring at the 3'-end of 18S pre-rRNA. However, the properties and activity of this complex are still poorly understood. We present here a detailed characterization of hNob1 organization and its interaction with hPno1. We redefine the boundaries of the endonuclease PIN domain present in hNob1 and we further delineate the precise interacting modules required for complex formation in hNob1 and hPno1. Altogether, our data contributes to a better understanding of the complex biology required during the site 3 cleavage step in ribosome biogenesis.

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Assembly and structure of the SSU processome — a nucleolar precursor of the small ribosomal subunit

Cited by 71 publications

References 50 publications

Good Vibrations: Structural Remodeling of Maturing Yeast Pre-40S Ribosomal Particles Followed by Cryo-Electron Microscopy

Good Vibrations: Structural Remodeling of Maturing Yeast Pre-40S Ribosomal Particles Followed by Cryo-Electron Microscopy

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

Domain definition and interaction mapping for the endonuclease complex hNob1/hPno1

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