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Related Experiment Videos

Mammalian Sec61 is associated with Sec62 and Sec63.

H A Meyer1, H Grau, R Kraft

  • 1Universität Göttingen, Zentrum Biochemie und Molekulare Zellbiologie, Biochemie II, Heinrich-Düker-Weg 12, Göttingen 37073, Germany.

The Journal of Biological Chemistry
|May 9, 2000
PubMed
Summary

Mammalian cells possess ribosome-free Sec61 complexes, involving new Sec62 and Sec63 proteins, for endoplasmic reticulum (ER) protein transport. This suggests a potential post-translational pathway distinct from yeast.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Trafficking

Background:

  • Protein transport across the endoplasmic reticulum (ER) membrane in yeast occurs via co-translational or post-translational pathways.
  • Mammalian protein translocation is primarily co-translational, relying on the ribosome-bound Sec61 complex.
  • The yeast post-translational pathway involves the Sec61p complex and the Sec62p-Sec63p subcomplex.

Purpose of the Study:

  • To investigate the existence and composition of non-ribosomal protein complexes involved in ER membrane transport in mammals.
  • To identify mammalian homologs of yeast Sec62p and Sec63p and characterize their association with the Sec61 complex.

Main Methods:

  • Primary sequence analysis of newly identified ER membrane proteins.
  • Identification and characterization of mammalian Sec61 complexes.

Related Experiment Videos

  • Comparative analysis with yeast protein transport mechanisms.

    • Main Results:

    • Discovery of ribosome-free mammalian Sec61 complexes associated with two novel ER membrane proteins.
    • Sequence homology confirms these proteins as mammalian Sec62 and Sec63, analogous to yeast Sec62p and Sec63p.
    • Mammalian ER membranes exhibit abundant Sec61-Sec62-Sec63 complexes, unlike yeast ER membranes.

    Conclusions:

    • Mammalian cells possess a distinct Sec61-Sec62-Sec63 complex, potentially mediating post-translational protein translocation.
    • This complex may represent an alternative or complementary pathway to the predominantly co-translational translocation in mammals.
    • The abundance of this complex suggests a significant role in mammalian ER protein transport, possibly compensating for less efficient post-translational activity compared to yeast.