The structural basis for mRNA recognition and cleavage by the ribosome-dependent endonuclease RelE

Cajetan Neubauer, Yong-Gui Gao, Kasper Røjkjær Andersen, Christine M Dunham, Ann C Kelley, Jendrik Hentschel, Kenn Gerdes, V Ramakrishnan, Ditlev E Brodersen

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    176 Citationer (Scopus)

    Abstract

    Translational control is widely used to adjust gene expression levels. During the stringent response in bacteria, mRNA is degraded on the ribosome by the ribosome-dependent endonuclease, RelE. The molecular basis for recognition of the ribosome and mRNA by RelE and the mechanism of cleavage are unknown. Here, we present crystal structures of E. coli RelE in isolation (2.5 A) and bound to programmed Thermus thermophilus 70S ribosomes before (3.3 A) and after (3.6 A) cleavage. RelE occupies the A site and causes cleavage of mRNA after the second nucleotide of the codon by reorienting and activating the mRNA for 2'-OH-induced hydrolysis. Stacking of A site codon bases with conserved residues in RelE and 16S rRNA explains the requirement for the ribosome in catalysis and the subtle sequence specificity of the reaction. These structures provide detailed insight into the translational regulation on the bacterial ribosome by mRNA cleavage.

    OriginalsprogEngelsk
    TidsskriftCell
    Vol/bind139
    Nummer6
    Sider (fra-til)1084-1095
    Antal sider12
    ISSN0092-8674
    DOI
    StatusUdgivet - 11 dec. 2009

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