Abstract
Production of small ribosomal subunits initially requires the formation of a 90S precursor followed by an enigmatic process of restructuring into the primordial pre-40S 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 90S pre-ribosome, followed by Utp24 endonuclease-driven RNA cleavage at site A(1), thereby separating the 5'-external transcribed spacer (ETS) from 18S ribosomal RNA. Next, the 5 '-ETS and 90S assembly factors become dislodged, but this occurs sequentially, not en bloc. Eventually, the primordial pre-40S emerges, still retaining some 90S factors including Dhr1, now ready to unwind the final small nucleolar U3-18S RNA hybrid. Our data shed light on the elusive 90S to pre-40S transition and clarify the principles of assembly and remodeling of large ribonucleoproteins.
Item Type: | Journal article |
---|---|
Faculties: | Chemistry and Pharmacy > Department of Biochemistry |
Subjects: | 500 Science > 540 Chemistry |
ISSN: | 0036-8075 |
Language: | English |
Item ID: | 89754 |
Date Deposited: | 25. Jan 2022, 09:32 |
Last Modified: | 25. Jan 2022, 09:32 |