Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Structural studies and the assembly of the heptameric post-translational translocon complex.

In Saccharomyces cerevisiae, some of the nascent chains can be post-translationally translocated into the endoplasmic reticulum through the heptameric post-translational translocon complex (post-translocon). This membrane-protein complex is composed of the protein-conducting channel and the tetrameric Sec62/63 complex. The Sec62/63 complex plays crucial roles in targeting of the signal recognition particle-independent protein substrate to the protein-conducting channel and in assembly of the post-translocon. Although the molecular mechanism of the post-translational translocation process has been well established, the structure of the post-translocon and how the channel and the Sec62/63 complex form the heptameric complex are largely uncharacterized. Here, we report a 20-Å resolution cryo-electron microscopy structure of the post-translocon. The purified post-translocon was found to have a mass of 287 kDa, which is consistent with the unit stoichiometry of the seven subunits as determined by a cysteine labeling experiment. We demonstrated that Triton X-100 dissociated the heptameric complex into three subcomplexes identified as the trimeric translocon Sec61-Sbh1-Sss1, the Sec63-Sec71-Sec72 trimer, and the heterotetramer Sec62-Sec63-Sec71-Sec72, respectively. Additionally, a role of the sixth cytosolic loop of Sec61 in assembly of the post-translocon was demonstrated. Mutations of conserved, positively charged amino acid residues in the loop caused decreased formation of the post-translocon. These studies provide the first architectural description of the yeast post-translocon.

Pubmed ID: 20826819


  • Harada Y
  • Li H
  • Wall JS
  • Li H
  • Lennarz WJ


The Journal of biological chemistry

Publication Data

January 28, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM33185
  • Agency: NIGMS NIH HHS, Id: GM74985

Mesh Terms

  • Cryoelectron Microscopy
  • Endoplasmic Reticulum
  • Membrane Transport Proteins
  • Multiprotein Complexes
  • Mutation
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Transport
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Structure-Activity Relationship