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Related Concept Videos

Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
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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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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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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.
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Author Spotlight: Quantitative Detection of DNA Protein Crosslinks and Their Post-Translational Modifications
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Post-translational modification of genetically encoded polypeptide libraries.

Alessandro Angelini1, Christian Heinis

  • 1Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.

Current Opinion in Chemical Biology
|April 15, 2011
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Summary
This summary is machine-generated.

Biological display systems and post-translational modification create diverse molecular libraries. Chemical strategies expand this diversity, enabling applications like biosensors and peptide-drug conjugates.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Synthetic Chemistry

Background:

  • Biological display systems facilitate the creation and screening of vast combinatorial molecular libraries.
  • Post-translational modification of encoded polypeptides generates chemical and structural diversity beyond linear polymers.

Purpose of the Study:

  • To review recent advancements in non-natural chemical strategies for post-translational modification of encoded polypeptide repertoires.
  • To highlight the application of these strategies in generating diverse molecules for various applications.

Main Methods:

  • Utilizing biological display systems for polypeptide library generation.
  • Applying post-translational modification strategies, including natural disulfide bond formation and various non-natural chemical methods.
  • Reviewing literature on the application of these modified polypeptides.

Main Results:

  • The first post-translational modification used was cysteine oxidation to form disulfide bridges for peptide cyclization.
  • Recent non-natural chemical strategies have been successfully applied to polypeptide repertoires.
  • These strategies enable the generation of optical biosensors, semisynthetic polypeptides, peptide-drug conjugates, and cyclic peptides.

Conclusions:

  • Post-translational modification significantly expands the chemical diversity of molecules generated via biological display systems.
  • Emerging chemical strategies offer powerful tools for creating novel molecular architectures with diverse functionalities.
  • These advancements pave the way for developing new therapeutics, diagnostics, and research tools.