A dominant mutation in the bacteriophage lambda S gene causes premature lysis and an absolute defective plating phenotype.
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The S and R genes of the bacteriophage lambda are required for lysis of the host. R encodes 'endolysin', a soluble transglycosylase which accumulates in the cytoplasm during late protein synthesis. S encodes a 'holin', a small membrane protein which, at a precisely scheduled time, terminates the vegetative cycle by forming a lethal lesion in the membrane through which gpR gains access to the peptidoglycan. A missense allele of S, Ala52Gly, causes lysis to occur prematurely at about 19-20 min after induction of a lysogen, compared to 45 min for the wild type. This allele has a severe plaque-forming defect which appears to be entirely a consequence of the early lysis and resultant severe reduction in particle burst size. The early-lysis phenotype is dominant and is aggravated, in terms of an even more reduced burst size, at both 30 degrees C and 42 degrees C. The mutation maps in the middle of a putative membrane-spanning helical domain of S, near the sites of other S- mutations with recessive non-lytic phenotypes. The mutation has no effect on S-protein accumulation or on the ratio of S107 and S105 products in the membrane. The mutation appears to affect the intrinsic timing function by which the S protein controls the lysis schedule.
author list (cited authors)
Johnson-Boaz, R., Chang, C. Y., & Young, R.
complete list of authors
Johnson-Boaz, R||Chang, CY||Young, R