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Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome.

Fernández IS, Bai XC, Murshudov G, Scheres SH, Ramakrishnan V - Cell (2014)

Bottom Line: By using recent advances in single-particle electron cryomicroscopy, we have solved the structure of CrPV-IRES bound to the ribosome of the yeast Kluyveromyces lactis in both the canonical and rotated states at overall resolutions of 3.7 and 3.8 Å, respectively.In both states, the pseudoknot PKI of the CrPV-IRES mimics a tRNA/mRNA interaction in the decoding center of the A site of the 40S ribosomal subunit.Translocation of the IRES by elongation factor 2 (eEF2) is required to bring the first codon of the mRNA into the A site and to allow the start of translation.

View Article: PubMed Central - PubMed

Affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.

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General Views of the CrPV-IRES/80S Complexes and Ratcheting Movements(A) Superposition of the canonical (yellow) and rotated (gray) states of the 40S subunit showing a counter-clockwise rotation.(B) Conformation of the CrPV-IRES in the rotated and canonical states of the ribosome in (A).(C) Interaction of the CrPV-IRES with the L1 stalk of the 60S subunit.(D) The conformation of the L1 stalk in different states of the ribosome. The stalk conformation with CrPV-IRES is from this work, whereas those with E-site tRNA and a hybrid P/E tRNA are from bacterial crystal structures (Gao et al., 2009; Tourigny et al., 2013).(E and F) Ribbon diagram (left) and schematic (right) showing the simultaneous interaction of CrPV-IRES with the L1 stalk in the 60S subunit and elements of the 40S subunit.
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fig2: General Views of the CrPV-IRES/80S Complexes and Ratcheting Movements(A) Superposition of the canonical (yellow) and rotated (gray) states of the 40S subunit showing a counter-clockwise rotation.(B) Conformation of the CrPV-IRES in the rotated and canonical states of the ribosome in (A).(C) Interaction of the CrPV-IRES with the L1 stalk of the 60S subunit.(D) The conformation of the L1 stalk in different states of the ribosome. The stalk conformation with CrPV-IRES is from this work, whereas those with E-site tRNA and a hybrid P/E tRNA are from bacterial crystal structures (Gao et al., 2009; Tourigny et al., 2013).(E and F) Ribbon diagram (left) and schematic (right) showing the simultaneous interaction of CrPV-IRES with the L1 stalk in the 60S subunit and elements of the 40S subunit.

Mentions: The rotated state of the ribosome differs from the canonical state by a counterclockwise rotation of the small subunit, including an additional movement of the head, as well as a movement of the L1 stalk (Figure 2A). Because the CrPV-IRES maintains interactions with each subunit in both states, the rotation of the subunits results in a somewhat different orientation and conformation for the CrPV-IRES in the two states (Figure 2B).


Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome.

Fernández IS, Bai XC, Murshudov G, Scheres SH, Ramakrishnan V - Cell (2014)

General Views of the CrPV-IRES/80S Complexes and Ratcheting Movements(A) Superposition of the canonical (yellow) and rotated (gray) states of the 40S subunit showing a counter-clockwise rotation.(B) Conformation of the CrPV-IRES in the rotated and canonical states of the ribosome in (A).(C) Interaction of the CrPV-IRES with the L1 stalk of the 60S subunit.(D) The conformation of the L1 stalk in different states of the ribosome. The stalk conformation with CrPV-IRES is from this work, whereas those with E-site tRNA and a hybrid P/E tRNA are from bacterial crystal structures (Gao et al., 2009; Tourigny et al., 2013).(E and F) Ribbon diagram (left) and schematic (right) showing the simultaneous interaction of CrPV-IRES with the L1 stalk in the 60S subunit and elements of the 40S subunit.
© Copyright Policy - CC BY
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4017093&req=5

fig2: General Views of the CrPV-IRES/80S Complexes and Ratcheting Movements(A) Superposition of the canonical (yellow) and rotated (gray) states of the 40S subunit showing a counter-clockwise rotation.(B) Conformation of the CrPV-IRES in the rotated and canonical states of the ribosome in (A).(C) Interaction of the CrPV-IRES with the L1 stalk of the 60S subunit.(D) The conformation of the L1 stalk in different states of the ribosome. The stalk conformation with CrPV-IRES is from this work, whereas those with E-site tRNA and a hybrid P/E tRNA are from bacterial crystal structures (Gao et al., 2009; Tourigny et al., 2013).(E and F) Ribbon diagram (left) and schematic (right) showing the simultaneous interaction of CrPV-IRES with the L1 stalk in the 60S subunit and elements of the 40S subunit.
Mentions: The rotated state of the ribosome differs from the canonical state by a counterclockwise rotation of the small subunit, including an additional movement of the head, as well as a movement of the L1 stalk (Figure 2A). Because the CrPV-IRES maintains interactions with each subunit in both states, the rotation of the subunits results in a somewhat different orientation and conformation for the CrPV-IRES in the two states (Figure 2B).

Bottom Line: By using recent advances in single-particle electron cryomicroscopy, we have solved the structure of CrPV-IRES bound to the ribosome of the yeast Kluyveromyces lactis in both the canonical and rotated states at overall resolutions of 3.7 and 3.8 Å, respectively.In both states, the pseudoknot PKI of the CrPV-IRES mimics a tRNA/mRNA interaction in the decoding center of the A site of the 40S ribosomal subunit.Translocation of the IRES by elongation factor 2 (eEF2) is required to bring the first codon of the mRNA into the A site and to allow the start of translation.

View Article: PubMed Central - PubMed

Affiliation: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge Biomedical Campus, Cambridge CB2 0QH, UK.

Show MeSH
Related in: MedlinePlus