Consistent mutational paths predict eukaryotic thermostability

BMC Evolutionary Biology

Peer Bork⁵  Ed Hurt²  Irmgard Sinning²  Daniel R Mende⁴  Sebastian Falk²  Chris Creevey³  Gert Bange¹  Stefan Amlacher²  Manimozhiyan Arumugam⁴  Bettina Bradatsch²  Vera van Noort⁴ 

[1] Current address: LOEWE Zentrum für synthetische Mikrobiologie, Phillips-University-Marburg, Marburg, Germany;Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg, D-69120, Germany;Teagasc Animal Bioscience Centre, Grange, Dunsany, Co. Meath, Ireland;European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, 69117, Germany;Max-Delbrück-Centre for Molecular Medicine, Berlin-Buch, Germany

关键词: Fungi;    Eukaryotes;    Protein engineering;    Comparative genomics;    Thermophily;   

Others  :  1130390
DOI  :  10.1186/1471-2148-13-7

 received in 2012-08-31, accepted in 2013-01-07,  发布年份 2013

【 摘 要 】

Background

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.

【 授权许可】

   
2013 van Noort et al.; licensee BioMed Central Ltd.

【 图 表 】

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