Bacteriophage φX1743D, a high temperature-resistant mutant of φX1743, was 10 times more stable than φX1743 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 φX1743 was changed to an α-helix in φX1743D. These results indicate that the temperature resistance of φX1743D may be caused by elevated hydrophobicity in the mutated region or by strong interaction between the mutated gene G protein and other capsid proteins.


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