The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis (Q27621393)

GOA release 2020-03-11

author name string

H Song

1

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P Mugnier

2

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A K Das

3

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H M Webb

4

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D R Evans

5

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M F Tuite

6

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B A Hemmings

7

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D Barford

Methods used in the structure determination of bovine mitochondrial F1 ATPase

8

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language of work or name

English

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publication date

4 February 2000

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published in

Cell

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volume

100

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page(s)

311-21

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issue

3

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cites work

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The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae

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Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner

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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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Peptide Chain Termination with Mammalian Release Factor

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Ribosomal binding site of release factors RF1 and RF2. A new translational termination assay in vitro

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The stretch of C-terminal acidic amino acids of translational release factor eRF1 is a primary binding site for eRF3 of fission yeast

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Release factors differing in specificity for terminator codons

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The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae

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Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3.

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