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Showing 1–12 of 12 results
Advanced filters: Author: Knud H Nierhaus Clear advanced filters

  • In this Review, Nierhaus and colleagues discuss the recent structural and mechanistic insights that have improved our understanding of elongation factor G (EF-G)-mediated forward-translocation and EF-4-mediated back-translocation on the bacterial ribosome.

    • Hiroshi Yamamoto
    • Yan Qin
    • Knud H. Nierhaus
    Reviews
    Nature Reviews Microbiology
    Volume: 12, P: 89-100

  • The ribosomal GTPase, LepA or EF4, can promote back-translocation of tRNAs, thus reversing translocation. The cryo-EM structure of the ribosome with EF4 now suggests how such back-translocation can be allowed to occur and reveals that the tRNA is in an intermediate state that deviates from its canonical position.

    • Sean R Connell
    • Maya Topf
    • Christian M T Spahn
    Research
    Nature Structural & Molecular Biology
    Volume: 15, P: 910-915

  • Stalled bacterial ribosomes can be rescued by interaction with SmpB protein and a highly structured transfer-messenger RNA, and a cryo-electron microscopy map of this complex now shows how EF-G-dependent translocation of this non-canonical ligand is facilitated by conformational changes in the ribosome and the transfer-messenger RNA.

    • David J. F. Ramrath
    • Hiroshi Yamamoto
    • Christian M. T. Spahn
    Research
    Nature
    Volume: 485, P: 526-529

  • Translocation is an essential step of protein synthesis in which the large tRNA2–mRNA complex inside the ribosome moves from the A and P sites to the P and E sites, respectively, bringing a new mRNA codon into the decoding center. This process is catalyzed by the elongation factor EF-G–GTP (eEF2 in eukaryotes) and is the least understood stage of peptide elongation. Four new reports describe the crystal structures of translocation intermediates, illustrating important details of the translocation reaction.

    • John Achenbach
    • Knud H Nierhaus
    News & Views
    Nature Structural & Molecular Biology
    Volume: 20, P: 1019-1022

  • Recruitment of elongation factor EF-G to the ribosome requires interaction between ribosomal proteins L12 and L11. New analyses identify a proline switch in L11, with the cis configuration allowing direct interaction between L11 and L12. EF-G has peptidyl-prolyl cis-trans isomerase activity driving the cis-trans isomerization of the proline switch, which might be a universal mechanism for efficient turnover of translational GTPases.

    • Li Wang
    • Fang Yang
    • Yan Qin
    Research
    Nature Structural & Molecular Biology
    Volume: 19, P: 403-410

  • A combined structural and biochemical analysis of an essential stress protein in Escherichia coli provides the first detailed insights into a bacterial translation mechanism designed to cope with cold shock conditions.

    • Daniel N Wilson
    • Knud H Nierhaus
    News & Views
    Nature Structural & Molecular Biology
    Volume: 11, P: 1026-1028

  • The structure of the archaeal toxin-antitoxin RelB–RelE complex offers surprises about resistance mechanisms and survival under stress conditions.

    • Daniel N Wilson
    • Knud H Nierhaus
    News & Views
    Nature Structural & Molecular Biology
    Volume: 12, P: 282-284