Topic
Lambda phage
About: Lambda phage is a research topic. Over the lifetime, 1609 publications have been published within this topic receiving 84675 citations. The topic is also known as: Enterobacteria phage lambda.
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TL;DR: This book describes the variety called λ and some of its relatives, which multiply in Escherichia coli, and explains how λ came to be the subject of intensive study.
Abstract: The bacteriophages form a diverse collection of viruses that multiply in bacterial cells. This book describes the variety called λ and some of its relatives, which multiply in Escherichia coli. Chapter 1 presents general characteristics of the λ group, and explains how λ came to be the subject of intensive study. The classical phages destroy their host cells by lysis. Lambda causes lysis too, but can also propagate in a form that permits joint multiplication of phage and host. Phages possessing this added potentiality are called temperate, in distinction from the broad class of intemperate or virulent species, which cannot reproduce without destroying their host cells. Lambda is also one of a few well known genetic elements, called episomes, that are able to multiply in the cell either autonomously or as part of the bacterial chromosome. In fact λ and the fertility agent F of E. coli are historical prototypes of the class. Campbell (1969) presents the comparative biology of episomes. For newcomers to phage research, Stent’s Molecular Biology of Bacterial Viruses (1963) can be recommended as a source book. THE LIFE CYCLE Lambda phage particles are about half protein and half DNA. Each contains one double-stranded DNA molecule encapsulated in an icosahedral head, 0.05 μ in diameter, from which projects a tubular tail, 0.15 μ long (Chapter 14). The DNA molecule is made from the usual four bases and weighs about 31 million daltons. Phage particles can be prepared in milligram quantities for analysis of various sorts. Lambda is...
35 citations
TL;DR: DNasel footprinting using either crude extracts or purified Fis indicate that binding on the left end of Mu occurs at a site which overlaps a weak transposase binding site, suggesting that Fis may modulate Mu growth by influencing the binding ofTransposase, or other proteins, to the transpos enzyme binding site(s), in a way similar to its influence on Xis binding in phage λ.
Abstract: We show, using gel retardation, that crude Escherichia coli cell extracts contain a protein which binds specifically to DNA fragments carrying either end of the phage Mu genome. We have identified this protein as Fis, a factor involved in several site-specific recombinational switches. Furthermore, we show that induction of a Mucts62 prophage in a fis lysogen occurs at a lower temperature than that of a wild-type strain, and that spontaneous induction of Mucts62 is increased in the fis mutant. DNasel footprinting using either crude extracts or purified Fis indicate that binding on the left end of Mu occurs at a site which overlaps a weak transposase binding site. Thus, Fis may modulate Mu growth by influencing the binding of transposase, or other proteins, to the transposase binding site(s), in a way similar to its influence on Xis binding in phage lambda.
35 citations
TL;DR: An Escherichia coli DNA fragment containing an Su+6 amber suppressor gene (supP) was cloned into a lambda gt lambda Ch vector by the shotgun method, selecting a Su+ 6 transducing phage lambda pSu+6 as a counterpart transduced phage carrying the wild-type allele.
35 citations
TL;DR: It was found that open complexes formed in the presence of cII protein were at least four times as stable as those formed in its absence, suggesting that RNA polymerase and cIIprotein may remain in close contact even after complexes are formed.
35 citations
TL;DR: The pst-2 pit double mutant was incapable of Pi utilization, but the phoT35 pits double mutant exhibited no such deficiency, and suggests that phosT35 lies in a different complementation group from phoS25 (Am) or pSt-2.
Abstract: Phosphate-specific transport system mutations phoT35, pst-2, and phoS25-(Am) were mapped between bgl and glmS, at about 83 min on the Escherichia coli chromosome. All three mutations were recessive to wild-type genes on transducing bacteriophage lambda asn. The phoS25 (Am) and pst-2 mutations were also recessive to transducing phage lambda dglm; however, the phoT35 mutation was not. This suggests that phoT35 lies in a different complementation group from phoS25 (Am) or pst-2. Isogenic series of strains carrying these mutations were constructed in two genetic backgrounds, pit+ (wild type) and pit (relying entirely on the phosphate-specific transport system for phosphate uptake). The pst-2 pit double mutant was incapable of Pi utilization, but the phoT35 pit double mutant exhibited no such deficiency.
35 citations