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Bhushan, S.* ; Meyer, H. ; Starosta, A.L.* ; Becker, T.* ; Mielke, T.* ; Berninghausen, O.* ; Sattler, M. ; Wilson, D.N.* ; Beckmann, R.*

Structural basis for translational stalling by human cytomegalovirus and fungal arginine attenuator peptide.

Mol. Cell 40, 138-146 (2010)

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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.

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Specific regulatory nascent chains establish direct interactions with the ribosomal tunnel, leading to translational stalling. Despite a wealth of biochemical data, structural insight into the mechanism of translational stalling in eukaryotes is still lacking. Here we use cryo-electron microscopy to visualize eukaryotic ribosomes stalled during the translation of two diverse regulatory peptides: the fungal arginine attenuator peptide (AAP) and the human cytomegalovirus (hCMV) gp48 upstream open reading frame 2 (uORF2). The C terminus of the AAP appears to be compacted adjacent to the peptidyl transferase center (PTC). Both nascent chains interact with ribosomal proteins L4 and L17 at tunnel constriction in a distinct fashion. Significant changes at the PTC were observed: the eukaryotic-specific loop of ribosomal protein L10e establishes direct contact with the CCA end of the peptidyl-tRNA (P-tRNA), which may be critical for silencing of the PTC during translational stalling. Our findings provide direct structural insight into two distinct eukaryotic stalling processes.

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