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Related Concept Videos

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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.
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In 1928, a German botanist Emil Heitz observed the moss nuclei with a DNA binding dye. He observed that while some chromatin regions decondense and spread out in the interphase nucleus, others do not. He termed them euchromatin and heterochromatin, respectively. He proposed that the heterochromatin regions reflect a functionally inactive state of the genome. It was later confirmed that heterochromatin is transcriptionally repressed, and euchromatin is transcriptionally active chromatin.
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Related Experiment Video

Updated: Feb 14, 2026

Measuring Peptide Translocation into Large Unilamellar Vesicles
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Positive zip coding in small protein translocation.

Yukari Okamoto1, Sojin Shikano2

  • 1From the Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, Illinois 60607-7170.

The Journal of Biological Chemistry
|February 21, 2018
PubMed
Summary

Small secretory proteins use a positively charged signal peptide for posttranslational translocation into the endoplasmic reticulum. This mechanism is crucial for proper protein secretion and linked to diabetes.

Keywords:
chargeendoplasmic reticulum (ER)positiveposttranslationalribosomesecretionsignal peptidesignal recognition particle (SRP)translocation

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Proteins entering the secretory pathway typically utilize signal peptides for translocation into the endoplasmic reticulum (ER).
  • The translocation mechanism for small polypeptides into the ER remains incompletely understood.

Purpose of the Study:

  • To elucidate the mechanism of ER translocation for small secretory proteins.
  • To investigate the role of signal peptide N-terminal charge in protein secretion.

Main Methods:

  • Analysis of posttranslational translocation of small secretory proteins.
  • Investigating the impact of N-terminal charge within the signal peptide.

Main Results:

  • A mechanism for posttranslational translocation of small secretory proteins involving a positive charge in the signal peptide N-terminal region was identified.
  • Defects in this positively charged element impair protein secretion.

Conclusions:

  • The N-terminal charge of signal peptides is critical for the posttranslational translocation of small secretory proteins.
  • Disruptions in this mechanism contribute to genetic mutations associated with diabetes.