RRC ID 30932
Author Takano K, Aoi A, Koga Y, Kanaya S.
Title Evolvability of thermophilic proteins from archaea and bacteria.
Journal Biochemistry
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.
Volume 52(28)
Pages 4774-80
Published 2013-7-16
DOI 10.1021/bi400652c
PMID 23822830
MeSH Archaeal Proteins / chemistry* Archaeal Proteins / genetics Bacterial Proteins / chemistry* Bacterial Proteins / genetics Directed Molecular Evolution* Models, Molecular Polymerase Chain Reaction Temperature
IF 2.997
Times Cited 6
DNA material Genomic DNA of Thermotoga maritima JCM 10099T (JGD07695)
General Microbes