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Consistent mutational paths predict eukaryotic thermostability

Vera van Noort1, Bettina Bradatsch2, Manimozhiyan Arumugam1, Stefan Amlacher2, Gert Bange25, Chris Creevey3, Sebastian Falk2, Daniel R Mende1, Irmgard Sinning2, Ed Hurt2* and Peer Bork14*

Author Affiliations

1 European Molecular Biology Laboratory, Meyerhofstrasse 1, Heidelberg, 69117, Germany

2 Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg, D-69120, Germany

3 Teagasc Animal Bioscience Centre, Grange, Dunsany, Co. Meath, Ireland

4 Max-Delbrück-Centre for Molecular Medicine, Berlin-Buch, Germany

5 Current address: LOEWE Zentrum für synthetische Mikrobiologie, Phillips-University-Marburg, Marburg, Germany

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BMC Evolutionary Biology 2013, 13:7  doi:10.1186/1471-2148-13-7

Published: 10 January 2013

Additional files

Additional file 1:

Table S1. Bacterial genomes and Optimal Growth Temperature. Table S2. Archaeal genomes and Optimal Growth Temperature. Table S3. correlations with OGT in bacterial and archaeal clades containing thermophiles. Figure S1. Phylogenetic tree of Sordariomycetes. A maximum likelihood tree was calculated with RaXML based on the concatenated alignments of 2,064 single copy orthologs in Sordariomycetes. Numbers on the branches indicate bootstrap support. Figure S2. Intergenic length distribution of N. crassa, C.globosum and C.thermophilum. Intergenic regions of C. thermophilum (blue) are significantly smaller than Neurospora crassa (red) and Chaetomium globosum (green), due to genome compaction. Figure S3. Thermostability of Wild-type and Mutant ctArx1. The critical temperature for thermostability is higher at lower protein concentration. The thermostability test (in vitro aggregation assay) with ctArx1 mutant proteins was performed at a 6-fold lower concentration (~1.3 mg/ml) than in Figure 4B ctArx1-nondestabilizing and ctArx1-destabilizing with five neutral or adaptive mutations, respectively (see Figure 4A, B ), and ctArx1 wild-type recombinant proteins were affinity-purified and incubated at the indicated temperatures for 1 hour, separated into supernatant (S) and pellet (P) fractions by centrifugation and subjected to SDS-PAGE and Coomassie stain in comparison to the input (I). PS: protein standard.

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