@ARTICLE{TreeBASE2Ref21503, author = {Vera van Noort and Bettina Bradatsch and Manimozhiyan Arumugam and Stefan Amlacher and Gert Bange and Chris Creevey and Sebastian Falk and Daniel R Mende and Irmgard Sinning and Ed Hurt and Peer Bork}, title = {Consistent mutational paths predict eukaryotic thermostability}, year = {2013}, keywords = {}, doi = {10.1186/1471-2148-13-7}, url = {http://}, pmid = {}, journal = {BMC Evolutionary Biology}, volume = {13}, number = {}, pages = {7}, abstract = {Proteomes of thermophilic prokaryotes have been instrumental in structural biology and successfully exploited in biotechnology, however many proteins required for eukaryotic cell function are absent from Bacteria or Archaea. With Chaetomium thermophilum, Thielavia terrestris and Thielavia heterothallica three genome sequences of thermophilic eukaryotes have been published. A phylogenetics-guided comparison of their proteomes with those of other, mesophilic Sordariomycetes revealed consistent amino acid substitutions associated to thermophily that were also present in an independent lineage of thermophilic fungi. The most consistent pattern is the substitution of lysine by arginine, which we could find in almost all lineages but has not been extensively used in protein stability engineering. By exploiting mutational paths towards the thermophiles, we could predict particular amino acid residues in individual proteins that contribute to thermostability and validated some of them experimentally. By determining the three-dimensional structure of an exemplar protein from C. Thermophilum (Arx1), we could also characterise the molecular consequences of some of these mutations. Thus, the comparative analysis of these three genomes not only enhances our understanding of the evolution of thermophily, but also provides new ways to engineer protein stability.} }

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