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Signal Sequences and Sorting Receptors01:41

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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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Targeting prion propagation using peptide constructs with signal sequence motifs.

Kajsa Löfgren Söderberg1, Peter Guterstam2, Ulo Langel2

  • 1The Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.

Archives of Biochemistry and Biophysics
|December 3, 2014
PubMed
Summary

Synthetic peptides targeting prion propagation show that specific signal peptides are crucial for anti-prion activity. Replacing the prion signal peptide with another, like NCAM11-19, retains efficacy, but conventional cell-penetrating peptides abolish the effect.

Keywords:
Cell penetrating peptidePolycationic motifPrionSignal peptide

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Synthetic peptides derived from the cellular prion protein (PrP(C)) N-terminus can inhibit prion propagation.
  • These anti-prion peptides possess cell-penetrating peptide (CPP) characteristics, featuring a prion protein hydrophobic signal sequence and a polycationic motif (KKRPKP).

Purpose of the Study:

  • To identify the essential sequence elements within KKRPKP-conjugates responsible for their anti-prion activity.
  • To investigate the role of the signal peptide and the polycationic motif in targeting prion propagation.

Main Methods:

  • Analysis of truncated and modified peptide constructs derived from mouse PrP(C) residues 1-28.
  • Testing peptide efficacy in prion-infected neuronal GT1-1 cells using prion strains RML and 22L.
  • Quantification of anti-prion effects by measuring the reduction of proteinase K resistant prions (PrP(Res)).

Main Results:

  • A 5-amino acid N-terminal shortening of the signal peptide abolished the anti-prion effect.
  • The PrP(C) signal peptide could be substituted with the signal peptide from Neural cell adhesion molecule-1 (NCAM11-19) while retaining anti-prion activity.
  • Conjugating the polycationic PrP(C)-motif to conventional CPPs (TAT48-60, transportan-10, penetratin) eliminated the anti-prion effect.

Conclusions:

  • The signal peptide sequence is critical for the anti-prion activity of KKRPKP-conjugates.
  • A non-prion signal peptide can mediate anti-prion effects, suggesting a generalizable mechanism.
  • The proposed mechanism involves signal peptide-mediated transport of the prion-binding motif to the Endosome Recycling Compartment to inhibit prion conversion.