The C-terminal helix of ribosomal P stalk recognizes a hydropobic groove of elongation factor 2 in a novel fashion

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Tanzawa, Takehito
Kato, Koji
Girodat, Dylan
Ose, Toyoyuki
Kumakura, Yuki
Weiden, Hans-Joachim
Uchiumi, Toshio
Tanaka, Isao
Yao, Min
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Oxford University Press
Archaea and eukaryotes have ribosomal P stalks composed of anchor protein P0 and aP1 homodimers (archaea) or P1•P2 heterodimers (eukaryotes). These P stalks recruit translational GTPases to the GTPase-associated center in ribosomes to provide energy during translation. The C-terminus of the P stalk is known to selectively recognize GTPases. Here we investigated the interaction between the P stalk and elongation factor 2 by determining the structures of P y ro c o c c u s h o r i ko s h i i EF-2 ( Pho EF2) in the Apo-form, GDP-form, GMPPCP-form (GTPform), and GMPPCP-form bound with 11 C-terminal residues of P1 (P1C11). Helical structured P1C11 binds to a hydrophobic groove between domain G and subdomain G of Pho EF-2, where is completely differentfromthatofaEF-1 in terms of both position and sequence, implying that such interaction characteristic may be requested by how GTPases perform their functions on the ribosome. Combining Pho EF2 P1-binding assays with a structural comparison of current Pho EF-2 structures and molecular dynamics model of a P1C11-bound GDP form, the conformational changes of the P1C11-binding groove in each form suggest that in response to the translation process, the groove has three states: closed, open, and release for recruiting and releasing GTPases
Sherpa Romeo green journal. Open access article. Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0) applies
C-terminal , Ribosomal P stalk , GTPases , Elongation factor
Tanzawa, T., Kato, K., Girodat, D., Ose, T., Kumakura, Y., Wieden, H.-J., ... Yao, M. (2018). The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion. Nucleic Acids Research, 46(6), 3232-3244. doi: 10.1093/nar/gky115