In pioneering work, a German-Japanese research team at BESSY II has been able to determine the 3D structure of a metalloprotein that plays an important role as a catalyst in all plant cells. This involves the DYW deaminase domain of what is referred to as the RNA editosome. The DYW domain alters messenger RNA nucleotides in chloroplasts and mitochondria and contains a zinc ion whose activity is controlled by a very unusual mechanism. The team has now been able to describe this mechanism in detail for the first time. Their study, published in Nature Catalysis, is considered a breakthrough in the field of plant molecular biology and has far-reaching implications for bioengineering.
All plant cells obtain their energy mainly from two organelles they contain – chloroplasts (responsible for photosynthesis) and mitochondria (responsible for the biochemical cycle of respiration that converts sugars into energy). However, a large number of a plant cell’s genes in its mitochondria and chloroplasts can develop defects, jeopardising their function. Nevertheless, plant cells evolved an amazing tool called the RNA editosome (a large protein complex) to repair these kinds of errors. It can modify defective messenger RNA that result from defective DNA by transforming (deamination) of certain mRNA nucleotides.
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Image: Around the catalytic centre is a group of molecules, the gating domain, which can occupy two different positions.
Credit: © M. Künsting / HZB