Evidence map›Paper›PMID 20826819›Full record

ArticleThe Journal of biological chemistry2011

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

Yoichiro Harada, Hua Li, Joseph S Wall, Huilin Li, William J Lennarz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

18 citing papers in PubMed, 40 citations in OpenAlex.

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  14. Protein translocation across the rough endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013
    Review
  15. Article
  16. Review
  17. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Yoichiro HaradaDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 11794, USA.
Hua Li
Joseph S Wall
Huilin Li
William J Lennarz
Stony Brook University · USBrookhaven National Laboratory · US

Funding

The structure and function of eukaryotic protein glycosylation enzymesR01CA231466 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI Huilin Li · 2018 to 2026
$4.0M
The Structural Basis of Eukaryotic Replication Origin Licensing by Cryo-EMR01GM074985 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI LI, HUILIN · 2006 to 2010
$1.7M
ENZYMATIC CONVERSION OF PROTEINS TO GLYCOPROTEINSR01GM033185 · NIGMS · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI LENNARZ, WILLIAM J · 1985 to 2007
$1.5M
ENZYMATIC CONVERSION OF PROTEINS TO GLYCOPROTEINSR37GM033185 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI LENNARZ, WILLIAM J · 1990 to 1999
–
NCI NIH HHS R01 CA231466NIGMS NIH HHS GM33185NIGMS NIH HHS GM74985NIGMS NIH HHS R01 GM033185NIGMS NIH HHS R01 GM074985NIGMS NIH HHS R37 GM033185
6 · The paper itself

Abstract

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.

Indexed as

Cryoelectron MicroscopyEndoplasmic ReticulumMembrane Transport ProteinsMultiprotein ComplexesMutationProtein Structure, QuaternaryProtein Structure, SecondaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipMembrane Transport ProteinsMultiprotein ComplexesSaccharomyces cerevisiae Proteins

Identifiers

PMID20826819
PMCPMC3024790
OpenAlexW1982296353

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.