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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

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Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Intrinsically Disordered Proteins02:18

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Translation01:31

Translation

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Lesson: Translation
Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of...
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Translation01:31

Translation

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Translation is the process of synthesizing proteins from the genetic information carried by messenger RNA (mRNA). Following transcription, it constitutes the final step in the expression of genes. This process is carried out by ribosomes, complexes of protein and specialized RNA molecules. Ribosomes, transfer RNA (tRNA), and other proteins produce a chain of amino acids—the polypeptide—as the end product of translation.
Translation Produces the Building Blocks of Life
Proteins are...
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Initiation of Translation02:33

Initiation of Translation

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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.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
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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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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Robustness by intrinsically disordered C-termini and translational readthrough.

April Snofrid Kleppe1, Erich Bornberg-Bauer1

  • 1Institute of Biodiversity and Evolution, University of Münster, Hüfferstr. 1, 48151 Münster, Germany.

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Summary

Translational readthrough (TR), a protein synthesis error, occurs in 5% of yeast genes. Highly expressed proteins prone to TR often have disordered C-termini, potentially mitigating negative effects.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Protein synthesis involves translating messenger RNA (mRNA) into protein chains.
  • Translational readthrough (TR) is an error where ribosomes bypass stop codons, extending proteins beyond their predicted length.
  • This phenomenon can introduce evolutionary constraints due to variations in protein sequence propensity for errors.

Purpose of the Study:

  • To investigate the frequency and characteristics of translational readthrough in Saccharomyces cerevisiae.
  • To identify features of proteins that are prone to or protected from translational readthrough.
  • To explore the evolutionary implications of translational readthrough.

Main Methods:

  • Analysis of ribosome profiling data in Saccharomyces cerevisiae.
  • Clustering of proteins based on their propensity for translational readthrough.
  • Comparative analysis of proteins prone and non-prone to TR.

Main Results:

  • Approximately 5% of yeast genes exhibit translational readthrough.
  • Proteins undergoing TR are frequently highly expressed.
  • Proteins prone to TR often possess intrinsically disordered C-termini.
  • Ribosomal subunit proteins are among those affected by TR.

Conclusions:

  • Highly expressed proteins may utilize intrinsically disordered C-termini to compensate for potential deleterious effects of translational readthrough.
  • Disordered C-termini may offer conformational flexibility without compromising native protein function.
  • Minimizing negative impacts of TR might also facilitate the exploration of protein isoform diversity and phenotypic landscapes.