Peptide bond formation destabilizes Shine-Dalgarno interaction on the ribosome
Article Abstract:
A study was conducted to compare the rupture force between ribosome complexes assembled on an mRNA with and without a strong Shine-Dalgarno (SD) sequence-a sequence found just upstream of the coding region of bacterial mRNAs involved in translation initiation. The removal of the SD sequence significantly reduced the rupture force in complexes carrying an aminoacyl tRNA, Phe-tRNA, in the A site, indicating that the SD interactions contribute significantly to the stability of the ribosomal complex on the mRNA before peptide bond formation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2007
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Real-time observation of trigger factor function on translating ribosomes
Article Abstract:
Fluorescence spectroscopy is used to monitor the ribosome-associated trigger factor (TF) function and structural rearrangements in real time in order to show that TF interacts with ribosomes and translating polypeptides in a dynamic reaction cycle. The results have described the way in which the TF prevents misfolding events during translation and have also provided a paradigm for the regulation of nucleotide-independent chaperones.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2006
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Release of eLF6 (p27(supra BBp)) from the 60s subunit allows 80s ribosome assembly
Article Abstract:
The 60S subunits of 80S ribosome are activated by release of eIF6(p27(supra BBp)) .The eIF6 release regulates subunit joining, and a physical and functional link is provided by RACK1 between PKC signaling and ribosome activation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
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