Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Insights into the structure of a protein transport assistant

15.01.2014
Proteins are the molecular building blocks and machines of the cell and are involved in virtually every process of life.

After protein production, many proteins are equipped with attachments such as sugar residues in order to perform their tasks properly. This process is directly coupled to the transport across a membrane.


Many protein complexes are involved in protein synthesis.Through the ER translocon (green, blue and red) the newly synthesized protein is transported across the membrane (gray).

Graphic: Friedrich Förster / Copyright: MPI of Biochemistry

Employing various methods of structural biology, scientists at the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich, Germany, have now gained insights into the architecture of the protein complex (ER translocon) responsible for this process. The results of the joint project have now been published in Nature Communications.

Producing a protein is a highly intricate process for the cell and involves many individual steps. Depending on the purpose for which a protein is used, there are different sites for protein production: the cytoplasm or the endoplasmic reticulum (ER). The ER is separated by a membrane from its surroundings in the cytoplasm. Even before protein synthesis is completed, the proteins produced at the ER enter via its membrane into the interior of the ER and are modified through the attachment of sugar residues concomitantly. Without these attachments, the proteins would not be able to fold properly and thus would not fulfill their functions in the cell.

Scientists of the research group “Modeling of Protein Complexes” have now described the architecture of the protein complex responsible for the transport and modification of the newly produced protein: the ER translocon. “It is located in the membrane of the ER, and this fact, together with its size and complex composition, has greatly hampered previous structural studies,” says Friedrich Förster, group leader at the MPI of Biochemistry, describing the initial situation. The structures of many subunits and their arrangement in the native ER translocon have thus far remained elusive.

It was not until cryoelectron tomography came into use that researchers could gain first insight into the architecture of the translocon. The sample is “shock frozen” to preserve its natural structure. Using an electron microscope, the scientists capture two-dimensional images of the object from different perspectives, from which they then reconstruct a three-dimensional image. Further investigations have made it possible to identify individual modules in the structure. Among them is the module that attaches the sugar residues to the newly produced protein.

“Based on this method, we will now try to determine the structure and location of other components of the ER translocon," says Förster. If the researchers know the individual structures of the ER translocon and their arrangement in the complex, they can indirectly draw conclusions about the precise functions and interactions of all components.

Original publication
Pfeffer, S., Dudek, J., Gogala, M., Schorr, S., Linxweiler, J., Lang, S., Becker, T., Beckmann, R., Zimmermann, R., Förster, F.: Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon. Nature Commun, January 10, 2014

Doi: 10.1038/ncomms4072 (2013).

Contact
Dr. Friedrich Förster
Modeling of Protein Complexes
Max Planck Institute of Biochemistry
Am Klopferspitz 18
82152 Martinsried
Germany
Email: foerster@biochem.mpg.de
http://www.biochem.mpg.de/foerster
Anja Konschak
Public Relations
Max Planck Institute of Biochemistry
Am Klopferspitz 18
82152 Martinsried
Germany
Tel. +49 89 8578-2824
E-Mail: konschak@biochem.mpg.de
http://www.biochem.mpg.de
Weitere Informationen:
http://www.biochem.mpg.de/foerster
- website of the research group "Modeling of Protein Complexes" (Friedrich Förster)
http://www.biochem.mpg.de/3686257/071_foerster_translocon_nature
- complete press release

Anja Konschak | Max-Planck-Institut
Further information:
http://www.biochem.mpg.de

More articles from Life Sciences:

nachricht Closing the carbon loop
08.12.2016 | University of Pittsburgh

nachricht Newly discovered bacteria-binding protein in the intestine
08.12.2016 | University of Gothenburg

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Significantly more productivity in USP lasers

In recent years, lasers with ultrashort pulses (USP) down to the femtosecond range have become established on an industrial scale. They could advance some applications with the much-lauded “cold ablation” – if that meant they would then achieve more throughput. A new generation of process engineering that will address this issue in particular will be discussed at the “4th UKP Workshop – Ultrafast Laser Technology” in April 2017.

Even back in the 1990s, scientists were comparing materials processing with nanosecond, picosecond and femtosesecond pulses. The result was surprising:...

Im Focus: Shape matters when light meets atom

Mapping the interaction of a single atom with a single photon may inform design of quantum devices

Have you ever wondered how you see the world? Vision is about photons of light, which are packets of energy, interacting with the atoms or molecules in what...

Im Focus: Novel silicon etching technique crafts 3-D gradient refractive index micro-optics

A multi-institutional research collaboration has created a novel approach for fabricating three-dimensional micro-optics through the shape-defined formation of porous silicon (PSi), with broad impacts in integrated optoelectronics, imaging, and photovoltaics.

Working with colleagues at Stanford and The Dow Chemical Company, researchers at the University of Illinois at Urbana-Champaign fabricated 3-D birefringent...

Im Focus: Quantum Particles Form Droplets

In experiments with magnetic atoms conducted at extremely low temperatures, scientists have demonstrated a unique phase of matter: The atoms form a new type of quantum liquid or quantum droplet state. These so called quantum droplets may preserve their form in absence of external confinement because of quantum effects. The joint team of experimental physicists from Innsbruck and theoretical physicists from Hannover report on their findings in the journal Physical Review X.

“Our Quantum droplets are in the gas phase but they still drop like a rock,” explains experimental physicist Francesca Ferlaino when talking about the...

Im Focus: MADMAX: Max Planck Institute for Physics takes up axion research

The Max Planck Institute for Physics (MPP) is opening up a new research field. A workshop from November 21 - 22, 2016 will mark the start of activities for an innovative axion experiment. Axions are still only purely hypothetical particles. Their detection could solve two fundamental problems in particle physics: What dark matter consists of and why it has not yet been possible to directly observe a CP violation for the strong interaction.

The “MADMAX” project is the MPP’s commitment to axion research. Axions are so far only a theoretical prediction and are difficult to detect: on the one hand,...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

ICTM Conference 2017: Production technology for turbomachine manufacturing of the future

16.11.2016 | Event News

Innovation Day Laser Technology – Laser Additive Manufacturing

01.11.2016 | Event News

#IC2S2: When Social Science meets Computer Science - GESIS will host the IC2S2 conference 2017

14.10.2016 | Event News

 
Latest News

Closing the carbon loop

08.12.2016 | Life Sciences

Applicability of dynamic facilitation theory to binary hard disk systems

08.12.2016 | Physics and Astronomy

Scientists track chemical and structural evolution of catalytic nanoparticles in 3-D

08.12.2016 | Materials Sciences

VideoLinks
B2B-VideoLinks
More VideoLinks >>>