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Printable Handouts
Navigable Slide Index
- Introduction
- Protein sorting
- Escherichia coli
- Post-translational targeting
- Co-translational targeting
- Evolutionary conserved translocons
- SecYEG heterotrimeric complex
- Purification of SecYEG complex
- Functional reconstitution of the SecYEG complex
- Structure of the SecYEG complex (1)
- Structure of the SecYEG complex (2)
- A model for signal peptide induced pore opening
- Oligomeric assemblies of the SecYEG complex
- SecYEG heterotrimers assemble into oligomers
- Ribosomes recruit purified Sec61 complexes
- SecYEG proteoliposomes
- Particle size of SecYEG in proteoliposomes
- SecA recruites SecYEG complexes into dimers
- Protein translocation intermediate trap SecYEG
- Cryo-EM of ribosome-associated Sec61 complex
- Cryo-EM of translating ribosome-associated Sec62
- Oligomeric state of the active SecYEG complex
- Monomers or tetramers?
- Challenges in cryo-EM analysis
- Cryo-EM of a ribosome dimeric SecYEG complex
- Orientation of SecYEG in dimeric complexes (1)
- Orientation of SecYEG in dimeric complexes (2)
- Back-to-back orientation in 2D crystals
- Back-to-back corresponds to an idle state
- Front-to-front orientation of ribosome-SecYEG
- A consolidated pore in the front-to-front
- Role of ribosome and SecA in channel opening
- Signal peptide induced open monomeric channel
- Mechanistic questions on a monomeric channel
- Interactions between SecYEG and the ribosome
- Two sites of interactions
- Model for co-translational translocation
- Post-translational translocation
- Domain structure of SecA
- SecA dimer structures
- Molecular docking of SecA-SecYEG
- Model for post-translational translocation
- Conclusion
- Acknowledgements
Topics Covered
- Bacterial protein sorting
- Evolutionary conserved translocons
- Structure of SecYEG complex
- Oligomeric assemblies of the SecYEG complex
- Oligomeric state of the active SecYEG complex
- Orientation of the SecYEG in dimeric complexes
- Active or passive role of ribosome and SecA during channel opening
Talk Citation
Driessen, A. (2021, March 3). Mechanism of translocon function: current insights and models [Video file]. In The Biomedical & Life Sciences Collection, Henry Stewart Talks. Retrieved November 23, 2024, from https://doi.org/10.69645/UQPT6727.Export Citation (RIS)
Publication History
Financial Disclosures
- Prof. Arnold Driessen has not informed HSTalks of any commercial/financial relationship that it is appropriate to disclose.
Update Available
The speaker addresses developments since the publication of the original talk. We recommend listening to the associated update as well as the lecture.
- Full lecture Duration: 74:44 min
- Update Interview Duration: 26:02 min
Mechanism of translocon function: current insights and models
A selection of talks on Biochemistry
Transcript
Please wait while the transcript is being prepared...
0:00
Hello, my name is Arnold Driessen.
I'm a professor at the Department of Molecular Microbiology
at the University of Groningen in the Netherlands.
Today, I would like to discuss with you the mechanism of translocon function,
in particular, current insights and models.
But before doing so,
let's first have a look at the organization of the eukaryotic cell.
0:22
This slide shows a typical scheme of a eukaryotic cell.
And all its membrane-bound organelles,
like for instance the vacuole, the peroxisome,
the mitochondria, the nucleus,
and the endoplasmic reticulum,
and many other organelles.
Each of these organelles contains specific subset of proteins,
which provides a specific function to this organelle.
Proteins are synthesized either on free ribosomes in the cytosol,
or on ribosomes bound to the endoplasmic reticulum.
These proteins, they need to end up at a specific localization,
and for that purpose, they contain specific labels, like for instance,
signal sequences that mediate targeting at the various organelles,
there are translocation machineries that translocate
these proteins from the cytosol into the organelle.
Proteins destined to be secreted are
synthesized on ribosomes bound to the endoplasmic reticulum.
Once they are translocated across the endoplasmic reticulum membrane,
they are sorted via vesicle sorting
route to the external medium and to the plasma membrane.
But if we now look at the bacterial cell, the left-hand corner,
we're struck by the simplicity of this bacterial cell.
In contrast to, for instance, a eukaryotic cell,
which may have up to 50 different organelles.
You observe a lesser complexity in compartmentalization in these bacteria.
Proteins are synthesized in the cytosol.
Some of these proteins have to function in the cytosol,
whereas others are targeted to the external organelles.
Like for instance, the inner membrane,
the periplasm which is the space in between the inner membrane and the outer membrane.
The outer membrane and the external medium.
These are also compartments,
and each of these compartments contains a specific subset of proteins
which provides a specific function to these compartments.
Even though we are dealing with less complexity,
the bacterial cell has to solve the same problem as a eukaryotic cell.
Proteins need to be targeted to specific compartments.