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6ZUO

Human RIO1(kd)-StHA late pre-40S particle, structural state A (pre 18S rRNA cleavage)

Summary for 6ZUO
Entry DOI10.2210/pdb6zuo/pdb
EMDB information11440
Descriptorpre-18S ribosomal RNA, 40S ribosomal protein S8, 40S ribosomal protein S9, ... (36 entities in total)
Functional Keywordshuman ribosome biogenesis, small ribosomal subunit, rrna processing, ribosome
Biological sourceHomo sapiens
More
Total number of polymer chains35
Total formula weight1284178.05
Authors
Plassart, L.,Shayan, R.,Plisson-Chastang, C. (deposition date: 2020-07-23, release date: 2021-05-12, Last modification date: 2024-05-01)
Primary citationPlassart, L.,Shayan, R.,Montellese, C.,Rinaldi, D.,Larburu, N.,Pichereaux, C.,Froment, C.,Lebaron, S.,O'Donohue, M.F.,Kutay, U.,Marcoux, J.,Gleizes, P.E.,Plisson-Chastang, C.
The final step of 40S ribosomal subunit maturation is controlled by a dual key lock.
Elife, 10:-, 2021
Cited by
PubMed Abstract: Preventing premature interaction of pre-ribosomes with the translation apparatus is essential for translational accuracy. Hence, the final maturation step releasing functional 40S ribosomal subunits, namely processing of the 18S ribosomal RNA 3' end, is safeguarded by the protein DIM2, which both interacts with the endoribonuclease NOB1 and masks the rRNA cleavage site. To elucidate the control mechanism that unlocks NOB1 activity, we performed cryo-electron microscopy analysis of late human pre-40S particles purified using a catalytically inactive form of the ATPase RIO1. These structures, together with in vivo and in vitro functional analyses, support a model in which ATP-loaded RIO1 cooperates with ribosomal protein RPS26/eS26 to displace DIM2 from the 18S rRNA 3' end, thereby triggering final cleavage by NOB1; release of ADP then leads to RIO1 dissociation from the 40S subunit. This dual key lock mechanism requiring RIO1 and RPS26 guarantees the precise timing of pre-40S particle conversion into translation-competent ribosomal subunits.
PubMed: 33908345
DOI: 10.7554/eLife.61254
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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數據於2024-11-06公開中

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