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dc.contributor.authorvan Noort, Vera
dc.contributor.authorBradatsch, Bettina
dc.contributor.authorArumugam, Manimozhiyan
dc.contributor.authorAmlacher, Stefan
dc.contributor.authorBange, Gert
dc.contributor.authorCreevey, Christopher J.
dc.contributor.authorFalk, Sebastian
dc.contributor.authorMende, Daniel R
dc.contributor.authorSinning, Irmgard
dc.contributor.authorHurt, Ed
dc.contributor.authorBork, Peer
dc.date.accessioned2013-05-21T15:18:38Z
dc.date.available2013-05-21T15:18:38Z
dc.date.issued2013-01-10
dc.identifier.citationVera van Noort, Bettina Bradatsch, Manimozhiyan Arumugam, Stefan Amlacher, Gert Bange, Chris Creevey, Sebastian Falk, Daniel R Mende, Irmgard Sinning, Ed Hurt and Peer Bork. Consistent mutational paths predict eukaryotic thermostability. BMC Evolutionary Biology 2013, 13:7 doi:10.1186/1471-2148-13-7en_GB
dc.identifier.issn1471-2148
dc.identifier.urihttp://hdl.handle.net/11019/403
dc.identifier.urihttp://dx.doi.org/10.1186/1471-2148-13-7
dc.identifier.urihttp://www.biomedcentral.com/1471-2148/13/7
dc.descriptionpeer-revieweden_GB
dc.descriptionpeer-reviewed
dc.description.abstractBackground: 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. Results: Studying the genomes and proteomes of these thermophilic fungi, we found common strategies of thermal adaptation across the different kingdoms of Life, including amino acid biases and a reduced genome size. A phylogenetics-guided comparison of thermophilic 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. Conclusions: 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.en_GB
dc.description.sponsorshipDeutsche Forschungsgemeinschaft (SFB 638/B2)en_GB
dc.language.isoenen_GB
dc.publisherBiomed Central
dc.relation.ispartofseriesBMC Evolutionary Biology;vol 13
dc.subjectThermophily
dc.subjectComparative genomics
dc.subjectProtein engineering
dc.subjectEukaryotes
dc.subjectFungi
dc.titleConsistent mutational paths predict eukaryotic thermostabilityen_GB
dc.typeArticleen_GB
refterms.dateFOA2018-01-12T08:00:53Z


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