The force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling
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چکیده
منابع مشابه
The force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling
Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ribosomal tunnel also provides a protected environment for initial protein folding events. Here, we present a 2.9 Å cryo-electron microscopy structure of a ribosome stalled during translation of the e...
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GTP hydrolysis, for the translocation of the mRNA chain and the tRNA molecules. Analysis of the three-dimensional structures of unbound ribosomal subunits from eubacteria (Figure 1A; Schluenzen et al., 2000; Wimberly et al., 2000; Harms et al., 2001) and archaea (Ban et al., 2000) as well as of the entire ribosome (Yusupov et al., 2001) clearly showed that the centers of the major ribosomal act...
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The mechanism of peptide bond synthesis constitutes a fundamental and long-debated question in molecular biology. For many years, ribosomologists championed a protein-based mechanism, similar to the charge relay system that has been proposed for peptide hydrolysis by serine proteinases [references in (1)]. As it has become apparent that the peptidyl transferase center is composed mainly of RNA,...
متن کاملMechanism of Ribosomal Peptide Bond Formation
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ژورنال
عنوان ژورنال: eLife
سال: 2017
ISSN: 2050-084X
DOI: 10.7554/elife.25642