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Structural basis for +1 ribosomal frameshifting during EF-G-catalyzed translocation
G. Demo, HB. Gamper, AB. Loveland, I. Masuda, CE. Carbone, E. Svidritskiy, YM. Hou, AA. Korostelev
Jazyk angličtina Země Velká Británie
Typ dokumentu časopisecké články, Research Support, N.I.H., Extramural, práce podpořená grantem
Grantová podpora
R01 AI139202
NIAID NIH HHS - United States
R35 GM127094
NIGMS NIH HHS - United States
R35 GM134931
NIGMS NIH HHS - United States
NLK
Directory of Open Access Journals
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od 2010
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od 2010-12-01
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od 2012
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od 2012
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od 2010-01-01
Open Access Digital Library
od 2015-01-01
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od 2015-01-01
Medline Complete (EBSCOhost)
od 2012-11-01
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od 2010-01-01
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- MeSH
- biokatalýza MeSH
- elektronová kryomikroskopie MeSH
- elongace translace peptidového řetězce genetika MeSH
- elongační faktor G chemie genetika metabolismus MeSH
- Escherichia coli genetika metabolismus MeSH
- konformace nukleové kyseliny MeSH
- konformace proteinů MeSH
- messenger RNA chemie genetika metabolismus MeSH
- molekulární modely MeSH
- posun čtecího rámce na ribozómech genetika MeSH
- proteiny z Escherichia coli chemie genetika metabolismus MeSH
- ribozomy genetika metabolismus ultrastruktura MeSH
- RNA ribozomální 16S chemie genetika metabolismus MeSH
- RNA transferová chemie genetika metabolismus MeSH
- tRNA-methyltransferasy genetika metabolismus MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, N.I.H., Extramural MeSH
Frameshifting of mRNA during translation provides a strategy to expand the coding repertoire of cells and viruses. How and where in the elongation cycle +1-frameshifting occurs remains poorly understood. We describe seven ~3.5-Å-resolution cryo-EM structures of 70S ribosome complexes, allowing visualization of elongation and translocation by the GTPase elongation factor G (EF-G). Four structures with a + 1-frameshifting-prone mRNA reveal that frameshifting takes place during translocation of tRNA and mRNA. Prior to EF-G binding, the pre-translocation complex features an in-frame tRNA-mRNA pairing in the A site. In the partially translocated structure with EF-G•GDPCP, the tRNA shifts to the +1-frame near the P site, rendering the freed mRNA base to bulge between the P and E sites and to stack on the 16S rRNA nucleotide G926. The ribosome remains frameshifted in the nearly post-translocation state. Our findings demonstrate that the ribosome and EF-G cooperate to induce +1 frameshifting during tRNA-mRNA translocation.
Central European Institute of Technology Masaryk University Brno Czech Republic
Department of Biochemistry and Molecular Biology Thomas Jefferson University Philadelphia PA USA
Citace poskytuje Crossref.org
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