|Title||90 pre-ribosome transformation into the primordial 40 subunit.|
|Journal, issue, pages||Science, Vol. 369, Issue 6510, Page 1470-1476, Year 2020|
|Publish date||Sep 18, 2020|
|Authors||Jingdong Cheng / Benjamin Lau / Giuseppe La Venuta / Michael Ameismeier / Otto Berninghausen / Ed Hurt / Roland Beckmann /|
|PubMed Abstract||Production of small ribosomal subunits initially requires the formation of a 90 precursor followed by an enigmatic process of restructuring into the primordial pre-40 subunit. We elucidate this ...Production of small ribosomal subunits initially requires the formation of a 90 precursor followed by an enigmatic process of restructuring into the primordial pre-40 subunit. We elucidate this process by biochemical and cryo-electron microscopy analysis of intermediates along this pathway in yeast. First, the remodeling RNA helicase Dhr1 engages the 90 pre-ribosome, followed by Utp24 endonuclease-driven RNA cleavage at site A, thereby separating the 5'-external transcribed spacer (ETS) from 18 ribosomal RNA. Next, the 5'-ETS and 90 assembly factors become dislodged, but this occurs sequentially, not en bloc. Eventually, the primordial pre-40 emerges, still retaining some 90 factors including Dhr1, now ready to unwind the final small nucleolar U3-18 RNA hybrid. Our data shed light on the elusive 90 to pre-40 transition and clarify the principles of assembly and remodeling of large ribonucleoproteins.|
|External links||Science / PubMed:32943521|
|Methods||EM (single particle)|
|Resolution||3.5 - 7.1 Å|
|Keywords||Cryoelectron Microscopy / DEAD-box RNA Helicases / ECM16 protein, S cerevisiae / Nuclear Proteins / PNO1 protein, S cerevisiae / Protein Conformation / RNA Cleavage / RNA, Ribosomal, 18S / Ribosomal Proteins / Ribosome Subunits, Large, Eukaryotic / Ribosome Subunits, Small, Eukaryotic / Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins / Utp24 protein, S cerevisiae / RIBOSOME / 90S pre-ribosome / 40S pre-ribosome / A1 cleavage / Dhr1|
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