In PLOS Biology this week you can read about a new General Ecosystem Model for predicting the effects of human activities, a global attempt to characterise a protein superfamily and new information about how a vital human transcription factor folds.
Human activities (such as climate change) are causing degradation of ecosystems at an unprecedented rate worldwide. One approach now commonly taken by scientists trying to understand these impacts is to model them mathematically. This week in PLOS Biology, Michael Harfoot, Drew Purves and colleagues make what is really the first attempt at modelling whole ecosystems mechanistically on a global scale – using their ‘General Ecosystem Model’ (GEM). It covers organisms of all sizes and can be simulated at any spatial scale from local to global. By using fundamental ecological processes experienced by all species (e.g. reproducing or being eaten), encoding them mathematically and then simulating the impacts of future scenarios, this GEM has the potential to help us manage key environmental issues better. The model is being released as open source code to allow it to be used and improved upon.
New research by Susan Mashiyama, Patricia Babbitt and colleagues sets out to revolutionise our knowledge of one of the great protein superfamilies: the cytosolic glutathione S-transferases (cytGSTs), whose main role involves making lipophilic (‘fat loving’) toxins soluble, so they can be attacked by other enzymes in the body. The authors made a systematic survey of the current knowledge of more than 13,000 cytGSTs, and then attempted to fill in the gaps regarding their structure and function. The resulting picture is dizzyingly complex, but represents an important first step for the work that lies ahead. Read more in the accompanying synopsis.
Stat3 is a transcription factor that is upregulated in some pathological conditions, including inflammatory diseases and cancer. Moses Kasembeli, David Tweardy and colleagues found that the folding and function of Stat3 are regulated by its interaction with TRiC – a type of protein called a chaperonin, which assist in the folding of other proteins. Manipulation of Stat3′s interaction with TRiC could be explored for therapeutic purposes.