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

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  • Cajetan Neubauer, MRC Laboratory of Molecular Biology, Cambridge, UK, Storbritannien
  • Yong-Gui Gao, Department of Biochemistry, Emory University School of Medicine, Atlanta, USA
  • Kasper Røjkjær Andersen
  • Christine M Dunham, Department of Biochemistry, Emory University School of Medicine, Atlanta, USA
  • Ann C Kelley, MRC Laboratory of Molecular Biology, Cambridge, UK, Storbritannien
  • Jendrik Hentschel, MRC Laboratory of Molecular Biology, Cambridge, UK, Storbritannien
  • Kenn Gerdes, Institute for Cell and Molecular Biosciences, The Medical School, University of Newcastle, Storbritannien
  • V Ramakrishnan, MRC Laboratory of Molecular Biology, Cambridge, UK, Storbritannien
  • Ditlev E Brodersen

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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