Evolution of Escherichia coli for growth at high temperatures.
Evolution depends on the acquisition of genomic mutations that increase cellular fitness. Here, we evolved Escherichia coli MG1655 cells to grow at extreme temperatures. We obtained a maximum growth temperature of 48.5 degrees C, which was not increased further upon continuous cultivation at this temperature for >600 generations. Despite a permanently induced heat shock response in thermoresistant cells, only exquisitely high GroEL/GroES levels are essential for growth at 48.5 degrees C. They depend on the presence of lysyl-tRNA-synthetase, LysU, because deletion of lysU rendered thermoresistant cells thermosensitive. Our data suggest that GroEL/GroES are especially required for the folding of mutated proteins generated during evolution. GroEL/GroES therefore appear as mediators of evolution of extremely heat-resistant E. coli cells.
Rudolph
Birgit
B
Department Chemie, Technische Universität München, Center for Integrated Protein Science Munich, 85747 Garching, Germany.
Gebendorfer
Katharina M
KM
Buchner
Johannes
J
Winter
Jeannette
J
D018835:Chaperonin 10 / Q000378:metabolism; D018834:Chaperonin 60 / Q000378:metabolism; D018833:Chaperonins / Q000737:chemistry; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D004926:Escherichia coli / Q000235:genetics*; D029968:Escherichia coli Proteins / Q000378:metabolism; D019143:Evolution, Molecular; D006360:Heat-Shock Proteins / Q000378:metabolism; D006358:Hot Temperature; D008954:Models, Biological; D009154:Mutation; D011506:Proteins / Q000737:chemistry; D040901:Proteomics / Q000379:methods; D013696:Temperature; D013997:Time Factors
D018835:Chaperonin 10; D018834:Chaperonin 60; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D011506:Proteins; D018833:Chaperonins
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