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

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dc.contributor.authorTanzawa, Takehito
dc.contributor.authorKato, Koji
dc.contributor.authorGirodat, Dylan
dc.contributor.authorOse, Toyoyuki
dc.contributor.authorKumakura, Yuki
dc.contributor.authorWeiden, Hans-Joachim
dc.contributor.authorUchiumi, Toshio
dc.contributor.authorTanaka, Isao
dc.contributor.authorYao, Min
dc.date.accessioned2019-12-18T22:11:30Z
dc.date.available2019-12-18T22:11:30Z
dc.date.issued2018
dc.descriptionSherpa Romeo green journal. Open access article. Creative Commons Attribution-NonCommercial 4.0 International License (CC BY-NC 4.0) appliesen_US
dc.description.abstractArchaea 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 GTPasesen_US
dc.description.peer-reviewYesen_US
dc.identifier.citationTanzawa, 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/gky115en_US
dc.identifier.urihttps://hdl.handle.net/10133/5637
dc.language.isoen_USen_US
dc.publisherOxford University Pressen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionHokkaido Universityen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.institutionNiigata Universityen_US
dc.publisher.urlhttps://doi.org/10.1093/nar/gky115en_US
dc.subjectC-terminal
dc.subjectRibosomal P stalk
dc.subjectGTPases
dc.subjectElongation factor
dc.titleThe C-terminal helix of ribosomal P stalk recognizes a hydropobic groove of elongation factor 2 in a novel fashionen_US
dc.typeArticleen_US
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