Journal article
Evolution of Protein Quaternary Structure in Response to Selective Pressure for Increased Thermostability
NJ Fraser, JW Liu, PD Mabbitt, GJ Correy, CW Coppin, M Lethier, MA Perugini, JM Murphy, JG Oakeshott, M Weik, CJ Jackson
Journal of Molecular Biology | Published : 2016
Abstract
Oligomerization has been suggested to be an important mechanism for increasing or maintaining the thermostability of proteins. Although it is evident that protein-protein contacts can result in substantial stabilization in many extant proteins, evidence for evolutionary selection for oligomerization is largely indirect and little is understood of the early steps in the evolution of oligomers. A laboratory-directed evolution experiment that selected for increased thermostability in the αE7 carboxylesterase from the Australian sheep blowfly, Lucilia cuprina, resulted in a thermostable variant, LcαE7-4a, that displayed increased levels of dimeric and tetrameric quaternary structure. A trade-off..
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Awarded by Defense Threat Reduction Agency
Funding Acknowledgements
C.J.J. thanks the Australian Research Council for a Future Fellowship. P.D.M. thanks the Science and Industry Endowment Fund for a John Stocker Fellowship. We acknowledge the La Trobe University-Comprehensive Proteomics Platform for access to essential equipment employed in this study. This work was supported by a grant from the USA Defense Threat Reduction Agency HDTRA1-11-C-0047. J.M.M. acknowledges additional support from NHMRC IRIISS grant 9000220 and the Victorian Government Operational Infrastructure Support scheme. We thank staff at the Australian Synchrotron SAXS beamline for help with data collection.