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

Takehito Tanzawa, Koji Kato, Dylan Girodat, Toyoyuki Ose, Yuki Kumakura, Hans Joachim Wieden, Toshio Uchiumi, Isao Tanaka, Min Yao

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

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 Pyrococcus horikoshii EF-2 (PhoEF-2) 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 PhoEF-2, where is completely different fromthat of aEF-1α 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 PhoEF- 2 P1-binding assays with a structural comparison of current PhoEF-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.

Original languageEnglish (US)
Pages (from-to)3232-3244
Number of pages13
JournalNucleic acids research
Volume46
Issue number6
DOIs
StatePublished - Jan 1 2018
Externally publishedYes

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Peptide Elongation Factor 2
GTP Phosphohydrolases
Pyrococcus horikoshii
Archaea
Eukaryota
Ribosomes
Myelin P0 Protein
Molecular Models
Molecular Dynamics Simulation

ASJC Scopus subject areas

  • Genetics

Cite this

The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion. / Tanzawa, Takehito; Kato, Koji; Girodat, Dylan; Ose, Toyoyuki; Kumakura, Yuki; Wieden, Hans Joachim; Uchiumi, Toshio; Tanaka, Isao; Yao, Min.

In: Nucleic acids research, Vol. 46, No. 6, 01.01.2018, p. 3232-3244.

Research output: Contribution to journalArticle

Tanzawa, T, Kato, K, Girodat, D, Ose, T, Kumakura, Y, Wieden, HJ, Uchiumi, T, Tanaka, I & 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, vol. 46, no. 6, pp. 3232-3244. https://doi.org/10.1093/nar/gky115
Tanzawa, Takehito ; Kato, Koji ; Girodat, Dylan ; Ose, Toyoyuki ; Kumakura, Yuki ; Wieden, Hans Joachim ; Uchiumi, Toshio ; Tanaka, Isao ; Yao, Min. / The C-terminal helix of ribosomal P stalk recognizes a hydrophobic groove of elongation factor 2 in a novel fashion. In: Nucleic acids research. 2018 ; Vol. 46, No. 6. pp. 3232-3244.
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