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Related Concept Videos

Cotranslational Protein Translocation01:20

Cotranslational Protein Translocation

Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Insertion of Single-pass Transmembrane Proteins in the RER01:26

Insertion of Single-pass Transmembrane Proteins in the RER

Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
Insertion of Multi-pass Transmembrane Proteins in the RER01:29

Insertion of Multi-pass Transmembrane Proteins in the RER

The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

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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Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
12:05

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies

Published on: March 6, 2013

Cis-trans peptide variations in structurally similar proteins.

Agnel Praveen Joseph1, Narayanaswamy Srinivasan, Alexandre G de Brevern

  • 1INSERM UMR-S 665, Dynamique des Structures et Interactions des Macromolécules Biologiques, Université Denis Diderot-Paris 7, INTS, 6 rue Alexandre Cabanel, Paris Cedex 15, France.

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Summary

Cis peptides, crucial for protein structure and function, are often not conserved in similar protein folds. These cis-trans conformation changes drive protein evolution and the emergence of new functions.

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Area of Science:

  • Structural Biology
  • Protein Chemistry
  • Evolutionary Biology

Background:

  • Cis peptides are vital for protein structural integrity and function.
  • Cis-trans peptide bond inter-conversion plays a key role in protein folding.

Purpose of the Study:

  • To analyze the conservation of cis peptides across similar protein folds.
  • To investigate amino acid preferences and local structural changes associated with cis-trans variations.

Main Methods:

  • Comparative analysis of cis peptide conservation in structurally related proteins.
  • Examination of amino acid propensities and local conformational changes.
  • Utilizing Protein Block-based description for backbone conformation analysis.

Main Results:

  • Approximately 34% of Xaa-Proline cis bonds are not conserved in related structures.
  • Glycine residues flanking peptide bonds show a higher propensity to adopt the trans conformation.
  • Over 30% of cis conformations in beta turns (types VIb and IV) are not conserved.
  • Local conformational changes associated with cis-trans variations differ significantly from general structural variations.

Conclusions:

  • Cis-trans peptide bond conversions are significant drivers of protein evolution.
  • These conformational changes facilitate the emergence of new functions, particularly in enzyme active sites.
  • Cis-trans conversions also play a role in inter-domain and inter-protein interactions.