Virulent mutants of phage P22

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Virulent mutants of bacteriophage p22.I. Isolation and genetic analysis.

Mutants of phage P22 which form plaques on a P22 lysogen have been isolated. These virulent mutants have been classified into three groups. (i) VirA mutants arise spontaneously in wild-type stocks and form very small turbid plaques on a P22 lysogen. The single mutation responsible for VirA virulence maps near the mnt locus, one of the immunity regions of phage P22. (ii) VirB mutants do not aris...

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Genetic properties of temperature-sensitive folding mutants of the coat protein of phage P22.

Temperature-sensitive mutations fall into two general classes: those generating thermolabile proteins; and those generating defects in protein synthesis, folding or assembly. Temperature-sensitive mutations at 17 sites in the gene for the coat protein of Phage P22 are of the latter class, preventing the productive folding of the polypeptide chain at restrictive temperature. We show here that, t...

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Synthesis and maturation of phage P22 DNA. II. Properties of temperature-sensitive phage mutants defective in DNA metabolism.

Three temperature-sensitive mutants of phage P22 have been isolated which are defective in phage DNA metabolism. After infection at restrictive temperature, one mutant (ts 12.1) fails to synthesize measurable quantities of phage DNA; nevertheless, parental phage DNA is recovered in a fast-sedimenting form similar to the first intermediate form observed after infection with normal phage. Another...

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Mutations of phage P22 affecting phage DNA synthesis and lysogenization.

Two temperature-sensitive mutants of phage P22, ts18.1 and ts12.1, are described which have recessive DNA-negative phenotypes. At high temperature they fail to synthesize phage DNA. In mixed infection with the two mutants or either mutant and wild-type phage, DNA synthesis and phage production are normal. In addition, under non-permissive conditions, these mutants fail to lysogenize and show do...

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Stem Mutants in the N-terminal Domain of the Phage P22 Tailspike Protein

The P22 tailspike protein is an intensely studied protein whose structure and sequence has been described. However, a study, describing important protein interactions related to its function at the N-terminal domain, has been lacking. The P22 tailspike protein (TSP) consists of three identical polypeptide chains of 666aa. The first 108 of the 666aa in the P22 TSP form a trimeric N-terminal doma...

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ژورنال

عنوان ژورنال: Virology

سال: 1972

ISSN: 0042-6822

DOI: 10.1016/0042-6822(72)90554-5