Abstract:
:Proteins from thermophiles possess high thermostability. The stabilization mechanisms differ between archaeal and bacterial proteins, whereby archaeal proteins are mainly stabilized via hydrophobic interactions and bacterial proteins by ion pairs. High stability is an important factor in promoting protein evolution, but the precise means by which different stabilization mechanisms affect the evolution process remain unclear. In this study, we investigated a random mutational drift of esterases from thermophilic archaea and bacteria at high temperatures. Our results indicate that mutations in archaeal proteins lead to improved function with no loss of stability, while mutant bacterial proteins are largely destabilized with decreased activity at high temperatures. On the basis of these findings, we suggest that archaeal proteins possess higher "evolvability" than bacterial proteins under temperature selection and are additionally able to evolve into eukaryotic proteins.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Takano K,Aoi A,Koga Y,Kanaya Sdoi
10.1021/bi400652csubject
Has Abstractpub_date
2013-07-16 00:00:00pages
4774-80issue
28eissn
0006-2960issn
1520-4995journal_volume
52pub_type
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