Gautsch J W, Wulff D L
Genetics. 1974 Jul;77(3):435-48. doi: 10.1093/genetics/77.3.435.
Six of seven hfl mutations of Escherichia coli K12, characterized by high frequencies of lysogenization by phage lambda and lambdacIII mutants, are shown to be tightly linked to, but not within, the purA locus. All six hfl mutations are recessive to wild type in hfl(+)/hfl merodiploids and all lie in a single complementation group, located just counterclockwise from the purA locus. All six mutations confer a slightly increased resistance to penicillin and rifamycin and a slightly increased sensitivity to sodium dodecyl sulfate. Some cases of intragenic complementation and intragenic recombination were observed. It is argued that the hfl(+) gene determines the synthesis of a protein which antagonizes lysogenization by phage lambda. It is further argued that the function of the lambdacIII gene product is to negate the antagonistic effect of this hfl(+) protein.
大肠杆菌K12的七个hfl突变中有六个，其特征是被噬菌体λ和λcIII突变体溶原化的频率很高，结果表明这些突变与purA基因座紧密连锁，但不在该基因座内。在hfl(+)/hfl部分二倍体中，所有六个hfl突变相对于野生型都是隐性的，并且都位于一个单一的互补群中，该互补群位于purA基因座的逆时针方向。所有六个突变对青霉素和利福霉素的抗性略有增加，对十二烷基硫酸钠的敏感性略有增加。观察到了一些基因内互补和基因内重组的情况。有人认为hfl(+)基因决定一种蛋白质的合成，这种蛋白质可拮抗噬菌体λ的溶原化。进一步有人认为，λcIII基因产物的功能是消除这种hfl(+)蛋白质的拮抗作用。
