
Full text loading...
Bacteriophage ϕX174am3trD a high temperature-resistant mutant of ϕX174am3, was 104 times more stable than 0 ϕX174am3 as judged by its survival ratio after heat treatment at 54 °C for 120 min. Complementation tests showed an involvement of gene G. Sequence analysis of this gene revealed three mutation sites, one transition and two insertions. The first was a silent mutation and the others brought about a change in one amino acid and an addition of another, respectively, in the gene G protein. These changes in amino acid sequence resulted in a change in the secondary structure of the protein. A β-turn region in part of the gene G protein of ϕX174am3 was changed to an α-helix in ϕX174am3trD These results indicate that the temperature resistance of ϕX174am3trD may be caused by elevated hydrophobicity in the mutated region or by strong interaction between the mutated gene G protein and other capsid proteins.
Article metrics loading...
Full text loading...
References
Data & Media loading...