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Related Concept Videos

Termination of Translation01:44

Termination of Translation

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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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Translation in Prokaryotes01:29

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Prokaryote translation is a complex, highly coordinated process that converts genetic information from mRNA into functional proteins. It involves three stages: initiation, elongation, and termination, each facilitated by specific molecular components.Initiation of TranslationThe process begins with the assembly of the ribosomal subunits and initiation factors on the mRNA. In bacteria, the 30S ribosomal subunit recognizes the Shine-Dalgarno sequence in the mRNA, a conserved region upstream of...
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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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Initiation of Translation02:33

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
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Structure of a human translation termination complex.

Sarah Matheisl1, Otto Berninghausen1, Thomas Becker1

  • 1Gene Center and Center for integrated Protein Science Munich, Department of Biochemistry, Feodor-Lynen-Str. 25, University of Munich, 81377 Munich, Germany.

Nucleic Acids Research
|September 19, 2015
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Summary

Eukaryotes use a single release factor, eRF1, to terminate protein translation. This study reveals the 3.8 Å structure of a human termination complex, showing how eRF1 recognizes stop codons through a unique U-turn conformation.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • Eukaryotes possess a single release factor, eRF1, responsible for recognizing all mRNA stop codons and hydrolyzing the peptidyl-tRNA bond.
  • Unlike bacteria with two release factors (RF1, RF2), the molecular mechanisms of eukaryotic termination complexes remain less understood due to a lack of high-resolution structural data.

Purpose of the Study:

  • To elucidate the high-resolution structure of a human translation termination complex.
  • To understand the molecular basis of stop codon recognition by the eukaryotic release factor eRF1.

Main Methods:

  • Cryo-electron microscopy was used to determine the 3.8 Å structure of a human translation termination complex.
  • A human cytomegalovirus (hCMV) stalling peptide was employed to stabilize the complex and inhibit eRF1's hydrolysis activity.

Main Results:

  • The structure reveals the human eRF1 bound to a UAA stop codon within the ribosome.
  • The UAA stop codon adopts a distinct U-turn conformation within a specific pocket formed by eRF1 and the ribosome.
  • This U-turn conformation is crucial for eRF1's ability to discriminate stop codons from sense codons.

Conclusions:

  • The study provides the first high-resolution structural insights into eukaryotic translation termination.
  • The unique U-turn conformation of the stop codon is key to its recognition by eRF1, highlighting a geometric surveillance mechanism.
  • This structural understanding rationalizes how eRF1 distinguishes between stop and sense codons during protein synthesis.