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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
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Transcriptional attenuation occurs when RNA transcription is prematurely terminated due to the formation of a terminator mRNA hairpin structure.  Bacteria use these hairpins to regulate the transcription process and control the synthesis of several amino acids including histidine, lysine, threonine, and phenylalanine. Transcription attenuation takes place in the non-coding regions of mRNA.
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Removal of an Internal Translational Start Site from mRNA While Retaining Expression of the Full-Length Protein
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Translational termination without a stop codon.

Nathan R James1, Alan Brown1, Yuliya Gordiyenko1

  • 1Medical Research Council (MRC) Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK.

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Summary
This summary is machine-generated.

Bacterial ribosomes can stall at the end of messenger RNA (mRNA). The alternative ribosome-rescue factor A (ArfA) rescues these nonstop complexes by recruiting release factor 2 (RF2).

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Bacterial Genetics

Background:

  • Ribosomes stall on messenger RNA (mRNA) lacking a stop codon, forming problematic nonstop complexes.
  • In bacteria, the alternative ribosome-rescue factor A (ArfA) is crucial for resolving these stalled ribosomes.

Purpose of the Study:

  • To elucidate the structural mechanism by which ArfA rescues bacterial nonstop ribosomes.
  • To understand how ArfA interacts with release factor 2 (RF2) and the ribosome.

Main Methods:

  • Electron cryomicroscopy (cryo-EM) was employed to determine high-resolution structures.
  • Structures captured ArfA bound to the ribosome with 3"-truncated mRNA.

Main Results:

  • ArfA binds within the ribosomal mRNA channel, acting as a substitute for the missing stop codon.
  • ArfA specifically recruits release factor 2 (RF2) into a compact, preaccommodated state.
  • The ArfA-bound RF2 conformation suggests a general mechanism for translational termination.

Conclusions:

  • ArfA facilitates translational termination by mimicking a stop codon and recruiting RF2.
  • A conformational switch in RF2, potentially triggered by ArfA, is key to peptide release.
  • This study reveals a conserved mechanism for ribosome rescue and translational termination in bacteria.