Structural basis for translation termination on the 70S ribosome (Q27651016)

1

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Haruichi Asahara

2

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Andrei Korostelev

3

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Jianyu Zhu

4

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Sergei Trakhanov

5

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Harry F Noller

Characterization of Three Proteins Involved in Polypeptide Chain Termination

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language of work or name

English

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publication date

14 August 2008

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published in

Nature

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volume

454

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issue

7206

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page(s)

852-7

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cites work

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Structure of the 70S ribosome complexed with mRNA and tRNA

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Two distinct conformations of the conserved RNA-rich decoding center of the small ribosomal subunit are recognized by tRNAs and release factors.

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Stop codon recognition by release factors induces structural rearrangement of the ribosomal decoding center that is productive for peptide release

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Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis.

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The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2

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Two distinct components of release factor function uncovered by nucleophile partitioning analysis

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A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis.

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The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis

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An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA.

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The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release

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