Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Cellular team players

30.06.2014

New insights into energy generation by heat shock protein Hsp90

Many enzymes work only with a co-trainer, of sorts. Scientists at the Technische Universitaet Muenchen (TUM) and the Cluster of Excellence Nanosystems Initiative Munich (NIM) show what this kind of cooperation looks like in detail using a novel methodology applied to the heat shock protein Hsp90.


Interaction of Hsp90 with P23 - Image: Bjoern Hellenkamp / TUM


FRET-Set-up in the laboratory - Photo: Christoph Ratzke / TUM

As in a successful football match, all actors in a cell must play in perfect coordination. A typical example for this kind of cooperation can be seen in the heat shock protein Hsp90, which controls the proper folding of other proteins. Together with a second molecule, the co-chaperone P23, it splits the energy source ATP to yield the energy it needs to do its work.

However, while normal enzyme reactions often are easy to follow because the involved proteins alter their conformations clearly, the interaction between P23 and ATP involves significantly less conspicuous changes in state.

... more about:
»ATP »Cellular »Cluster »FRET »Hsp90 »NIM »TUM »enzyme »fluorescent »heat »proteins »shock

Using a sophisticated methodology, a team led by Professor Thorsten Hugel, head of the Research Group for Molecular Machines at the TU München and member of the Cluster of Excellence Nanosystems Initiative Munich (NIM), has now managed to observe this reaction in detail for the first time – step for step with single molecules of Hsp90, P23 and ATP.

Live transmission of molecular processes

To this end, the team adapted the so-called FRET (Foerster resonance energy transfer) methodology to suit their requirements. The approach works by using a variety of fluorescent dye molecules bonded to specific sites in the involved components. When these complexes are excited with light of a specific wavelength, the pigments start to fluoresce in a kind of chain reaction. The emitted fluorescent light reveals the precise distance between the marked sites, right down to the nanometer.

To determine exactly how the components Hsp90, P23 and ATP interact with each other, the biophysicists observed the positions and bonding sequences of the individual molecules over a span of several minutes. From the resulting data they could deduce even the smallest of changes, as well as the biological function of the overall complex.

Energy production only as a team

Using this approach, the Munich researchers successfully demonstrated in detail that the P23 protein strengthens ATP bonding, thereby significantly increasing the amount of energy exploited. They also showed that the two substances bond with Hsp90 this effectively only as a team, thereby allowing ATP splitting to be used so successful.

“Without P23 the heat shock enzyme effectively runs on idle,” explains Bjoern Hellenkamp the results. “When P23 joins the game, it is like shifting into gear. The energy is released and the reaction moves clearly in one direction. This is referred to as directionality.”

In the near future the biophysicists want to investigate in detail how Hsp90 uses the exploited energy. The newly established methodology also allows them to investigate other multicomponent systems with mechanisms that have eluded study because of their minimal conformational alterations.

Publication:

Four-colour FRET reveals directionality in the Hsp90 multicomponent machinery
C. Ratzke, B. Hellenkamp, T. Hugel
Nature Communications 5, Article number: 4192. Published online: 20 June 2014
DOI: 10.1038/ncomms5192

Contact:

Prof. Dr. Thorsten Hugel
Technische Universitaet Muenchen (TUM)
Physik-Department E40
James Franck-Str. 1, 85748 Garching, Germany
E-mail - Telefon: +49 89 289 16781Internet

Andreas Battenberg | Technische Universität München
Further information:
http://www.tum.de/en/about-tum/news/press-releases/short/article/31639/

Further reports about: ATP Cellular Cluster FRET Hsp90 NIM TUM enzyme fluorescent heat proteins shock

More articles from Life Sciences:

nachricht The birth of a new protein
20.10.2017 | University of Arizona

nachricht Building New Moss Factories
20.10.2017 | Albert-Ludwigs-Universität Freiburg im Breisgau

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Neutron star merger directly observed for the first time

University of Maryland researchers contribute to historic detection of gravitational waves and light created by event

On August 17, 2017, at 12:41:04 UTC, scientists made the first direct observation of a merger between two neutron stars--the dense, collapsed cores that remain...

Im Focus: Breaking: the first light from two neutron stars merging

Seven new papers describe the first-ever detection of light from a gravitational wave source. The event, caused by two neutron stars colliding and merging together, was dubbed GW170817 because it sent ripples through space-time that reached Earth on 2017 August 17. Around the world, hundreds of excited astronomers mobilized quickly and were able to observe the event using numerous telescopes, providing a wealth of new data.

Previous detections of gravitational waves have all involved the merger of two black holes, a feat that won the 2017 Nobel Prize in Physics earlier this month....

Im Focus: Smart sensors for efficient processes

Material defects in end products can quickly result in failures in many areas of industry, and have a massive impact on the safe use of their products. This is why, in the field of quality assurance, intelligent, nondestructive sensor systems play a key role. They allow testing components and parts in a rapid and cost-efficient manner without destroying the actual product or changing its surface. Experts from the Fraunhofer IZFP in Saarbrücken will be presenting two exhibits at the Blechexpo in Stuttgart from 7–10 November 2017 that allow fast, reliable, and automated characterization of materials and detection of defects (Hall 5, Booth 5306).

When quality testing uses time-consuming destructive test methods, it can result in enormous costs due to damaging or destroying the products. And given that...

Im Focus: Cold molecules on collision course

Using a new cooling technique MPQ scientists succeed at observing collisions in a dense beam of cold and slow dipolar molecules.

How do chemical reactions proceed at extremely low temperatures? The answer requires the investigation of molecular samples that are cold, dense, and slow at...

Im Focus: Shrinking the proton again!

Scientists from the Max Planck Institute of Quantum Optics, using high precision laser spectroscopy of atomic hydrogen, confirm the surprisingly small value of the proton radius determined from muonic hydrogen.

It was one of the breakthroughs of the year 2010: Laser spectroscopy of muonic hydrogen resulted in a value for the proton charge radius that was significantly...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

ASEAN Member States discuss the future role of renewable energy

17.10.2017 | Event News

World Health Summit 2017: International experts set the course for the future of Global Health

10.10.2017 | Event News

Climate Engineering Conference 2017 Opens in Berlin

10.10.2017 | Event News

 
Latest News

Terahertz spectroscopy goes nano

20.10.2017 | Information Technology

Strange but true: Turning a material upside down can sometimes make it softer

20.10.2017 | Materials Sciences

NRL clarifies valley polarization for electronic and optoelectronic technologies

20.10.2017 | Interdisciplinary Research

VideoLinks
B2B-VideoLinks
More VideoLinks >>>