Show simple item record

dc.contributor.author
Ameismeier, Michael
dc.contributor.author
Zemp, Ivo
dc.contributor.author
van den Heuvel, Jasmin
dc.contributor.author
Thoms, Matthias
dc.contributor.author
Berninghausen, Otto
dc.contributor.author
Kutay, Ulrike
dc.contributor.author
Beckmann, Roland
dc.date.accessioned
2020-12-03T10:38:36Z
dc.date.available
2020-12-02T05:44:07Z
dc.date.available
2020-12-03T10:38:36Z
dc.date.issued
2020-11-26
dc.identifier.issn
0028-0836
dc.identifier.issn
1476-4687
dc.identifier.other
10.1038/s41586-020-2929-x
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/454079
dc.description.abstract
Eukaryotic ribosomes consist of a small 40S and a large 60S subunit that are assembled in a highly coordinated manner. More than 200 factors ensure correct modification, processing and folding of ribosomal RNA and the timely incorporation of ribosomal proteins1,2. Small subunit maturation ends in the cytosol, when the final rRNA precursor, 18S-E, is cleaved at site 3 by the endonuclease NOB13. Previous structures of human 40S precursors have shown that NOB1 is kept in an inactive state by its partner PNO14. The final maturation events, including the activation of NOB1 for the decisive rRNA-cleavage step and the mechanisms driving the dissociation of the last biogenesis factors have, however, remained unresolved. Here we report five cryo-electron microscopy structures of human 40S subunit precursors, which describe the compositional and conformational progression during the final steps of 40S assembly. Our structures explain the central role of RIOK1 in the displacement and dissociation of PNO1, which in turn allows conformational changes and activation of the endonuclease NOB1. In addition, we observe two factors, eukaryotic translation initiation factor 1A domain-containing protein (EIF1AD) and leucine-rich repeat-containing protein 47 (LRRC47), which bind to late pre-40S particles near RIOK1 and the central rRNA helix 44. Finally, functional data shows that EIF1AD is required for efficient assembly factor recycling and 18S-E processing. Our results thus enable a detailed understanding of the last steps in 40S formation in human cells and, in addition, provide evidence for principal differences in small ribosomal subunit formation between humans and the model organism Saccharomyces cerevisiae.
en_US
dc.language.iso
en
en_US
dc.publisher
Nature
dc.title
Structural basis for the final steps of human 40S ribosome maturation
en_US
dc.type
Journal Article
dc.date.published
2020-11-18
ethz.journal.title
Nature
ethz.journal.volume
587
en_US
ethz.journal.issue
7835
en_US
ethz.pages.start
683
en_US
ethz.pages.end
687
en_US
ethz.grant
Ribosome synthesis in mammalian cells
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
London
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::03543 - Kutay, Ulrike / Kutay, Ulrike
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::03543 - Kutay, Ulrike / Kutay, Ulrike
ethz.grant.agreementno
166565
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
Projekte Lebenswissenschaften
ethz.date.deposited
2020-12-02T05:44:26Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Metadata only
en_US
ethz.rosetta.installDate
2020-12-03T10:38:50Z
ethz.rosetta.lastUpdated
2022-03-29T04:09:48Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.atitle=Structural%20basis%20for%20the%20final%20steps%20of%20human%2040S%20ribosome%20maturation&rft.jtitle=Nature&rft.date=2020-11-26&rft.volume=587&rft.issue=7835&rft.spage=683&rft.epage=687&rft.issn=0028-0836&1476-4687&rft.au=Ameismeier,%20Michael&Zemp,%20Ivo&van%20den%20Heuvel,%20Jasmin&Thoms,%20Matthias&Berninghausen,%20Otto&rft.genre=article&rft_id=info:doi/10.1038/s41586-020-2929-x&
 Search print copy at ETH Library

Files in this item

FilesSizeFormatOpen in viewer

There are no files associated with this item.

Publication type

Show simple item record