Insights into translational termination from the structure of RF2 bound to the ribosome.

نویسندگان

  • Albert Weixlbaumer
  • Hong Jin
  • Cajetan Neubauer
  • Rebecca M Voorhees
  • Sabine Petry
  • Ann C Kelley
  • Venki Ramakrishnan
چکیده

The termination of protein synthesis occurs through the specific recognition of a stop codon in the A site of the ribosome by a release factor (RF), which then catalyzes the hydrolysis of the nascent protein chain from the P-site transfer RNA. Here we present, at a resolution of 3.5 angstroms, the crystal structure of RF2 in complex with its cognate UGA stop codon in the 70S ribosome. The structure provides insight into how RF2 specifically recognizes the stop codon; it also suggests a model for the role of a universally conserved GGQ motif in the catalysis of peptide release.

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منابع مشابه

How do the ends replicate?

20 Schmeing, T.M. et al. (2005) An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438, 520–524 21 Weixlbaumer, A. et al. (2008) Insights into translational termination from the structure of RF2 bound to the ribosome. Science 322, 953–956 22 Laurberg, M. et al. (2008) Structural basis for translation termination on the 70S ribosome. Nature...

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A Posttermination Ribosomal Complex Is the Guanine Nucleotide Exchange Factor for Peptide Release Factor RF3

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Crystal Structures of the Ribosome in Complex with Release Factors RF1 and RF2 Bound to a Cognate Stop Codon

During protein synthesis, translational release factors catalyze the release of the polypeptide chain when a stop codon on the mRNA reaches the A site of the ribosome. The detailed mechanism of this process is currently unknown. We present here the crystal structures of the ribosome from Thermus thermophilus with RF1 and RF2 bound to their cognate stop codons, at resolutions of 5.9 Angstrom and...

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Crystal structure of the 70S ribosome bound with the Q253P mutant form of release factor RF2.

Bacterial translation termination is mediated by release factors RF1 and RF2, which recognize stop codons and catalyze hydrolysis of the peptidyl-tRNA ester bond. The catalytic mechanism has been debated. We proposed that the backbone amide NH group, rather than the side chain, of the glutamine of the universally conserved GGQ motif participates in catalysis by H-bonding to the tetrahedral tran...

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Crystal structure of a translation termination complex formed with release factor RF2.

We report the crystal structure of a translation termination complex formed by the Thermus thermophilus 70S ribosome bound with release factor RF2, in response to a UAA stop codon, solved at 3 A resolution. The backbone of helix alpha5 and the side chain of serine of the conserved SPF motif of RF2 recognize U1 and A2 of the stop codon, respectively. A3 is unstacked from the first 2 bases, conta...

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عنوان ژورنال:
  • Science

دوره 322 5903  شماره 

صفحات  -

تاریخ انتشار 2008