Journal: Nature / Year: 2006 Title: Hrr25-dependent phosphorylation state regulates organization of the pre-40S subunit. Authors: Thorsten Schäfer / Bohumil Maco / Elisabeth Petfalski / David Tollervey / Bettina Böttcher / Ueli Aebi / Ed Hurt / Abstract: The formation of eukaryotic ribosomes is a multistep process that takes place successively in the nucleolar, nucleoplasmic and cytoplasmic compartments. Along this pathway, multiple pre-ribosomal ...The formation of eukaryotic ribosomes is a multistep process that takes place successively in the nucleolar, nucleoplasmic and cytoplasmic compartments. Along this pathway, multiple pre-ribosomal particles are generated, which transiently associate with numerous non-ribosomal factors before mature 60S and 40S subunits are formed. However, most mechanistic details of ribosome biogenesis are still unknown. Here we identify a maturation step of the yeast pre-40S subunit that is regulated by the protein kinase Hrr25 and involves ribosomal protein Rps3. A high salt concentration releases Rps3 from isolated pre-40S particles but not from mature 40S subunits. Electron microscopy indicates that pre-40S particles lack a structural landmark present in mature 40S subunits, the 'beak'. The beak is formed by the protrusion of 18S ribosomal RNA helix 33, which is in close vicinity to Rps3. Two protein kinases Hrr25 and Rio2 are associated with pre-40S particles. Hrr25 phosphorylates Rps3 and the 40S synthesis factor Enp1. Phosphorylated Rsp3 and Enp1 readily dissociate from the pre-ribosome, whereas subsequent dephosphorylation induces formation of the beak structure and salt-resistant integration of Rps3 into the 40S subunit. In vivo depletion of Hrr25 inhibits growth and leads to the accumulation of immature 40S subunits that contain unstably bound Rps3. We conclude that the kinase activity of Hrr25 regulates the maturation of 40S ribosomal subunits.
History
Deposition
Mar 29, 2006
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Header (metadata) release
Apr 3, 2006
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Map release
Jun 1, 2006
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Update
Oct 17, 2012
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Current status
Oct 17, 2012
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 295 K / Instrument: HOMEMADE PLUNGER Details: Vitrification instrument: Plunger with environmental chamber Method: Blot for 15 s with Whatman No 1
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Electron microscopy
Microscope
FEI/PHILIPS CM200FEG
Temperature
Average: 94 K
Alignment procedure
Legacy - Astigmatism: bjective lens astigmatism was corrected at
Image recording
Category: CCD / Film or detector model: GENERIC CCD / Digitization - Sampling interval: 14 µm / Number real images: 69 / Bits/pixel: 12
Tilt angle min
0
Tilt angle max
0
Electron beam
Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
236 out of 400 classes were used for final reconstruction
CTF correction
Details: Each Particle
Final reconstruction
Applied symmetry - Point group: C1 (asymmetric) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 32.0 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: IMAGIC 5 Details: reconstructions were calculated from half of the class averages. Euler angles of class averages were determined by projection matching Number images used: 4827
Final angle assignment
Details: IMAGIC
Final two d classification
Number classes: 236
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