Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Molecular high-speed Origami - Researchers elucidate important mechanism of protein folding

09.05.2014

Proteins are responsible for nearly every essential process of life. Their form and structure are of crucial importance for their functionality.

Scientists at the Max Planck Institute of Biochemistry (MPIB) have recently discovered a so far unknown sequence of reactions which is necessary for newly generated proteins to acquire their correct structure.


GroEL/ES nano-cage (light blue and white) with encapsulated substrate protein (orange).

Image: Andreas Bracher / Copyright: MPI of Biochemistry

„In the mechanism we found, the folding is accomplished in a number of fast intermediate steps rather than in one single block“, explains Manajit Hayer-Hartl, MPIB research group leader. „Because this mode of action is energetically more favorable, the proteins are folded not only correctly, but also much faster than previously assumed.“

Proteins are the workhorses of the cell and thus responsible for almost all biological functions including metabolism, signal transmission or the determination of the cell’s shape. However, before they can fulfill their various tasks, the chain-like molecules must first adopt an intricate three-dimensional conformation. This process is called protein folding and is one of the most important processes in biology.

In fact, in the event of improper folding, proteins are often no more able to carry out their duties, or even tend to clump together in aggregates. This in turn can lead to severe diseases like Alzheimer’s or Parkinson’s. In order to avoid this, specialized proteins, the so-called chaperones, help other proteins to adopt their proper shape.

The bacterial chaperones GroEL and GroES serve as an example for this principle: together, they build up a cage-like structure in which they encapsulate new, not yet folded proteins, thereby al-lowing them to fold properly. However, the exact way in which this is accomplished has so far been unclear and is a research topic of the MPIB team led by Manajit Hayer-Hartl and F. Ulrich Hartl, in collaboration with John Engen from Northeastern University in Boston.

Active acceleration of folding
„Our results demonstrate that the chaperones not only prevent protein clumping, but also dramatically accelerate the folding process”, explains Florian Georgescauld, scientist at the MPIB. „Surprisingly, the chaperones achieve this by changing the mechanism of folding: Instead of folding in one large single block, the protein gets its final structure in a series of small, rapid steps – like an elaborate high-speed Origami.” The researchers think that splitting up the reaction might render it energetically more favorable, which in turn would lead to increased speed. Hence, the folding process is finished in a few seconds rather than in several minutes.

The study shows for the first time that chaperones can act not only passively, by preventing aggregation, but as an active folding cage that catalyzes the folding process. This results in a high-speed folding mechanism which is of particular biological relevance, so the researchers say, since in this way proteins can be folded faster than they are produced. Thus, a backlog of proteins which are not yet or improperly folded and the disastrous consequences which might go along with this can be avoided.
[HS]

Original Publication:
F. Georgescauld, K. Popova, A. J. Gupta, A. Bracher, J. R. Engen, M. Hayer-Hartl and F. U. Hartl: GroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain Folding. Cell, May 8, 2014.
DOI: 10.1016/j.cell.2014.03.038

Contact:
Dr. Manajit Hayer-Hartl
Chaperonin-assisted Protein Folding
Max Planck Institute of Biochemistry
Am Klopferspitz 18
82152 Martinsried
Germany
E-Mail: mhartl@biochem.mpg.de
http://www.biochem.mpg.de/hayer-hartl

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/news

Weitere Informationen:

http://www.biochem.mpg.de/news/ueber_das_institut/forschungsbereiche/strukturforschung/hayer_hartl_press - Press Page of the Research Group "Chaperonin-assisted Protein Folding" (Manajit Hayer-Hartl)
http://www.biochem.mpg.de/en/rg/hayer-hartl - Website of the Research Group "Chaperonin-assisted Protein Folding" (Manajit Hayer-Hartl)

Anja Konschak | Max-Planck-Institut

More articles from Life Sciences:

nachricht Warming ponds could accelerate climate change
21.02.2017 | University of Exeter

nachricht An alternative to opioids? Compound from marine snail is potent pain reliever
21.02.2017 | University of Utah

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Breakthrough with a chain of gold atoms

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

Im Focus: DNA repair: a new letter in the cell alphabet

Results reveal how discoveries may be hidden in scientific “blind spots”

Cells need to repair damaged DNA in our genes to prevent the development of cancer and other diseases. Our cells therefore activate and send “repair-proteins”...

Im Focus: Dresdner scientists print tomorrow’s world

The Fraunhofer IWS Dresden and Technische Universität Dresden inaugurated their jointly operated Center for Additive Manufacturing Dresden (AMCD) with a festive ceremony on February 7, 2017. Scientists from various disciplines perform research on materials, additive manufacturing processes and innovative technologies, which build up components in a layer by layer process. This technology opens up new horizons for component design and combinations of functions. For example during fabrication, electrical conductors and sensors are already able to be additively manufactured into components. They provide information about stress conditions of a product during operation.

The 3D-printing technology, or additive manufacturing as it is often called, has long made the step out of scientific research laboratories into industrial...

Im Focus: Mimicking nature's cellular architectures via 3-D printing

Research offers new level of control over the structure of 3-D printed materials

Nature does amazing things with limited design materials. Grass, for example, can support its own weight, resist strong wind loads, and recover after being...

Im Focus: Three Magnetic States for Each Hole

Nanometer-scale magnetic perforated grids could create new possibilities for computing. Together with international colleagues, scientists from the Helmholtz Zentrum Dresden-Rossendorf (HZDR) have shown how a cobalt grid can be reliably programmed at room temperature. In addition they discovered that for every hole ("antidot") three magnetic states can be configured. The results have been published in the journal "Scientific Reports".

Physicist Dr. Rantej Bali from the HZDR, together with scientists from Singapore and Australia, designed a special grid structure in a thin layer of cobalt in...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Booth and panel discussion – The Lindau Nobel Laureate Meetings at the AAAS 2017 Annual Meeting

13.02.2017 | Event News

Complex Loading versus Hidden Reserves

10.02.2017 | Event News

International Conference on Crystal Growth in Freiburg

09.02.2017 | Event News

 
Latest News

Impacts of mass coral die-off on Indian Ocean reefs revealed

21.02.2017 | Earth Sciences

Novel breast tomosynthesis technique reduces screening recall rate

21.02.2017 | Medical Engineering

Use your Voice – and Smart Homes will “LISTEN”

21.02.2017 | Trade Fair News

VideoLinks
B2B-VideoLinks
More VideoLinks >>>