Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Fusion protein controls design of photosynthesis platform

13.05.2015

Collaborative project uncovers the role of a protein in the formation and maintenance of the inner membrane structures of photosynthetic systems

Chloroplasts are the solar cells of plants and green algae. In a process called photosynthesis, light energy is used to produce biochemical energy and the oxygen we breathe. Thus, photosynthesis is one of the most important biological processes on the planet.


An IM30 ring docks with internal membranes. In the background is part of an image of a blue-green alga prepared using an electron microscope. A 3D model of the IM30 ring can be seen in the foreground. The images are not to scale.

Source: Dirk Schneider and Jürgen Markl

A central part of photosynthesis takes place in a specialized structure within chloroplasts, the thylakoid membrane system. Despite its apparent important function, until now it was not clear how this specialized internal membrane system is actually formed.

In a collaborative project, researchers at Johannes Gutenberg University Mainz (JGU) in Germany have now identified how this membrane is generated. According to their findings, a protein called IM30 plays a major role by triggering the fusion of internal membranes. The study elucidating the role of IM30 involved biologists, chemists, biochemists, and biophysicists at Mainz University and the Max Planck Institute for Polymer Research. Their results have recently been published in the journal Nature Communications.

Chloroplasts are organelles found in higher plants and green algae. They contain an internal membrane system, so-called thylakoid membranes, where the key processes of photosynthesis take place. "A detailed understanding of photosynthesis and the associated molecular processes is essential to properly comprehend life on our planet," emphasized Professor Dirk Schneider of the Institute of Pharmaceutical Sciences and Biochemistry at JGU, who coordinated the study.

"Despite the significance of the process, we know almost nothing about how these special membranes are formed and maintained." It had not previously been possible to identify a single fusion-mediating protein in photosynthetic cells, even though it was perfectly clear that such proteins have to be involved in the development of thylakoid membranes.

With this in mind, the Mainz-based research team isolated and investigated the protein IM30 from a blue-green alga, which might be classified as a "free-living chloroplast." IM30 – the "IM" stands for "internal membrane" while 30 is its atomic mass (30 kilodaltons) – was first described in the mid-1990s and it was demonstrated that it binds to internal membranes.

Thanks to the combined expertise of the teams headed by Professor Dirk Schneider, Professor Jürgen Markl of the JGU Institute of Zoology, and Professor Tobias Weidner of the Max Planck Institute for Polymer Research it has now emerged that IM30 forms a ring structure that specifically interacts with phospholipids of the membranes.

"This binding alters the membrane structure and under certain conditions can lead to membrane fusion," explained Schneider. In absence of IM30, thylakoid membranes are noticeably deteriorated, which can subsequently lead to loss of cell viability. The IM30 fusion protein provides a starting point for future research, unraveling new types of membrane fusion mechanisms in chloroplasts and blue-green algae.

The interdisciplinary research project was primarily undertaken by doctoral candidates at the Max Planck Graduate Center (MPGC). The MPGC was founded in June 2009 to support joint projects and shared doctorates at Johannes Gutenberg University Mainz and the Max Planck Institutes for Polymer Research and for Chemistry, both of which are based in Mainz.

Publication:
Raoul Hennig et al.
IM30 triggers membrane fusion in cyanobacteria and chloroplasts
Nature Communications, 8. Mai 2015
DOI: 10.1038/ncomms8018

Further information:
Professor Dr. Dirk Schneider
Institute of Pharmaceutical Sciences and Biochemistry – Therapeutic Life Sciences
Johannes Gutenberg University Mainz (JGU)
55099 Mainz, GERMANY
phone +49 6131 39-25833
fax +49 6131 39-25348
e-mail: dirk.schneider@uni-mainz.de
http://www.bio.chemie.uni-mainz.de/46.php

Weitere Informationen:

http://www.uni-mainz.de/presse/18298_ENG_HTML.php - press release ;
http://www.bio.chemie.uni-mainz.de/46.php – Prof. Dirk Schneider ;
http://www.bio.uni-mainz.de/zoo/312_DEU_HTML.php – Prof. Jürgen Markl ;
http://www.mpip-mainz.mpg.de/~weidner – Prof. Tobias Weidner ;
http://www.nature.com/naturecommunications – Nature Communications

Petra Giegerich | idw - Informationsdienst Wissenschaft

More articles from Life Sciences:

nachricht Zap! Graphene is bad news for bacteria
23.05.2017 | Rice University

nachricht Discovery of an alga's 'dictionary of genes' could lead to advances in biofuels, medicine
23.05.2017 | University of California - Los Angeles

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Turmoil in sluggish electrons’ existence

An international team of physicists has monitored the scattering behaviour of electrons in a non-conducting material in real-time. Their insights could be beneficial for radiotherapy.

We can refer to electrons in non-conducting materials as ‘sluggish’. Typically, they remain fixed in a location, deep inside an atomic composite. It is hence...

Im Focus: Wafer-thin Magnetic Materials Developed for Future Quantum Technologies

Two-dimensional magnetic structures are regarded as a promising material for new types of data storage, since the magnetic properties of individual molecular building blocks can be investigated and modified. For the first time, researchers have now produced a wafer-thin ferrimagnet, in which molecules with different magnetic centers arrange themselves on a gold surface to form a checkerboard pattern. Scientists at the Swiss Nanoscience Institute at the University of Basel and the Paul Scherrer Institute published their findings in the journal Nature Communications.

Ferrimagnets are composed of two centers which are magnetized at different strengths and point in opposing directions. Two-dimensional, quasi-flat ferrimagnets...

Im Focus: World's thinnest hologram paves path to new 3-D world

Nano-hologram paves way for integration of 3-D holography into everyday electronics

An Australian-Chinese research team has created the world's thinnest hologram, paving the way towards the integration of 3D holography into everyday...

Im Focus: Using graphene to create quantum bits

In the race to produce a quantum computer, a number of projects are seeking a way to create quantum bits -- or qubits -- that are stable, meaning they are not much affected by changes in their environment. This normally needs highly nonlinear non-dissipative elements capable of functioning at very low temperatures.

In pursuit of this goal, researchers at EPFL's Laboratory of Photonics and Quantum Measurements LPQM (STI/SB), have investigated a nonlinear graphene-based...

Im Focus: Bacteria harness the lotus effect to protect themselves

Biofilms: Researchers find the causes of water-repelling properties

Dental plaque and the viscous brown slime in drainpipes are two familiar examples of bacterial biofilms. Removing such bacterial depositions from surfaces is...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

AWK Aachen Machine Tool Colloquium 2017: Internet of Production for Agile Enterprises

23.05.2017 | Event News

Dortmund MST Conference presents Individualized Healthcare Solutions with micro and nanotechnology

22.05.2017 | Event News

Innovation 4.0: Shaping a humane fourth industrial revolution

17.05.2017 | Event News

 
Latest News

Scientists propose synestia, a new type of planetary object

23.05.2017 | Physics and Astronomy

Zap! Graphene is bad news for bacteria

23.05.2017 | Life Sciences

Medical gamma-ray camera is now palm-sized

23.05.2017 | Medical Engineering

VideoLinks
B2B-VideoLinks
More VideoLinks >>>