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Protein evolution follows a modular principle
Date:7/23/2014

This news release is available in German.

Proteins impart shape and stability to cells, drive metabolic processes and transmit signals. To perform these manifold tasks, they fold into complex three-dimensional shapes. Scientists at the Max Planck Institute for Developmental Biology in Tbingen have now discovered that proteins can be constructed of similar amino acid chains even when their three-dimensional shapes differ significantly. This suggests that the proteins that exist today arose from common precursors. Presumably, in the course of evolution they were built up from smaller fragments according to a modular principle.

Proteins consist of long chains of 20 different amino acid building blocks that fold into a characteristic three-dimensional structure. It is noteworthy that some modules, known as protein domains, occur more frequently than others. Scientists suspect that many of these domains share a common evolutionary origin.

To test this theory, the Max Planck researchers focussed on two large, evolutionarily ancient protein groups that differ significantly in their folding pattern. While "flavodoxin-like" protein domains fold into a kind of sandwich shape, so-called (βα)8-barrel proteins stack two sandwich elements on top of each other to form a barrel-like structure. "In the folded state it's very difficult to recognize similarities between these two types," Jos Arcadio Faras Rico, first author of the study, explains. The Tbingen scientists therefore compared the amino acid chains of over a thousand representatives of both folding types in a computer analysis. They found that short, characteristic sequences of amino acids occur in both folding types.

In the next step, the team identified a third folding type whose amino acid sequence
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Contact: Nadja Winter
presse-eb@tuebingen.mpg.de
49-707-160-1444
Max-Planck-Gesellschaft
Source:Eurekalert  

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