The article “Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions” has been published today in Science!
Most proteins assemble into complexes to achieve a specific biological function. In this work, we show how small Heat Shock Proteins assemble selectively according to mechanisms away from the typical shape and charge complementarity, and that this phenomenon might in fact be widespread. Our results indicate an economical mechanism for duplicated proteins to evolve distinct functions: modification of a minimal amount of amino acids, altering protein dynamics but not their structure, allows preventing co-assembly.
This work is the fruit of several years of collaboration between researchers from areas as diverse as molecular and plant biology, molecular dynamics and modelling and crystallography. For more information, see the University of Oxford blog post.
Georg K. A. Hochberg et al., Structural principles that enable oligomeric small heat-shock protein paralogs to evolve distinct functions, Science, Vol. 359, Issue 6378, pp. 930-935, 2018 [Supplemental data is available here]