Exploring the speed of protein assembly – University of Copenhagen

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08 December 2017

Exploring the speed of protein assembly

Grant

Independent Research Fund Denmark has awarded researchers at Copenhagen Plant Science Centre a grant for studying the assembly of photosynthetic protein complexes in plants.

Photosynthesis in plants is responsible for the production of both the organic carbons and the oxygen, on which all life on Earth depends. The molecular structures of the photosynthetic complexes in plants are known in great detail. However our understanding of how the many chlorophyll and electron transfer co-factors are incorporated into the photosynthetic complexes is still rudimentary.

Researchers at Copenhagen Plant Science Centre have received funding from the Independent Research Fund Denmark for the project “Co-translational insertion of co-factors into photosystems”. The aim of the project is to fill the knowledge gap and help us understand the molecular basis for assembly of the photosynthetic complexes.

Photosystem II. Picture by Neveu, Curtis, via Wikimedia Commons.

The project will focus on proteins in the two photosystems in plants. These protein molecules are quite complex. Photosystem I consists of 12 proteins and 123 co-factors while photosystem II is made up of 20 proteins and 51 co-factors. The accurate assembly of the complex protein molecules is necessary for them to function in the right way in the plant.

In the plant cell, the ribosome is a kind of protein factory that builds proteins, and different co-factors are added along the way. The speed of the building process varies and we think this might be of importance to the correct attachment of the co-factors. Part of our experiment will be to slow down and speed up the protein building process to see if this affects how the proteins are put together correctly, says postdoc Lars Scharff from Copenhagen Plant Science Centre.

In a longer perspective the project will lead to a better understanding of how nature makes the photosystems correctly. The researchers will get a broader knowledge about how large protein complexes are made and will thus be able to design and engineer them more efficiently in the future. This could also be relevant for protein complexes in other organisms such as the mitochondrion and in bacteria.