A Genetic Switch: Phage Lambda Revisited
The first edition of Mark Ptashne's 1986 book describing the principles of gene regulation in phage lambda became a classic in both content and form, setting a standard of clarity and precise prose that has rarely been bettered. This edition is a reprint of the original text, together with a new chapter updating the story to 2004. Among the striking new developments are recent findings on longā€“range interactions between proteins bound to widely separated sites on the phage genome, and a detailed description of how gene activation works.
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A repressor dimer binds through its amino domains to a 17 base pair
There are three 17 base pair repressor binding sites in the right operator
Cro binds first to O3 then to O 1 and O2 thereby first turning off
Other editions - View all
Acad activator adjacent affinity amino acids amino domain bacterial bacterium base pairs bearing begin transcription Biol bound carboxyl domain cells Chapter cl gene cleavage cleaves coli cooperative binding Cro bind curve described DNA molecule DNA-binding DNA-bound efficiently encoding enzyme example experiment gene expression gene regulation genetic half-site helices helix immune inactivated induce infection interactions IPTG irradiation kcal lac repressor Lambda LexA linker lyse lysogen lytic growth major groove merase methylation monomers mRNA mutant Natl nonspecific o-helix octamer operator sites P22 repressor Pabo pathway phage chromosome phage genes plaque plasmid polymerase bind positive control Proc promoter prophage protease protein-DNA Ptashne RecA recognition helix region regulatory protein repres repression repressor and Cro repressor at O2 repressor concentration repressor dimer binds repressor monomers residues RNA polymerase sequence shown in Figure shows specific strand structure subunit surface switch tein tetramers tion transcribed turns vitro vivo wild-type X chromosome
Page 141 - Other examples of the contribution of secondary products to chemosystematics can be found in the references cited at the end of the chapter but this is an area in which there is great scope for further research.
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Page 105 - Ingles. 1985. Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases. Cell 42:599-610.
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Page 105 - DNase footprinting: a simple method for the detection of protein-DNA binding specificity. Nucl. Acids. Res.
Page 137 - DL (2001). Bacteriophage lambda: Alive and well and still doing its thing. Curr. Opin. Microbiol 4, 201-207. 2. Hendrix, RW, Roberts, JW, Stahl, JW, and Weisberg, RA (Eds.) (1983). Lambda II. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY. 3. Ptashne, M. (1992). "A Genetic Switch,
Page 29 - R. 1983. Represser and Cro protein: Structure, function, and role in lysogenization. In Lambda II, ed.
Page 105 - Maximizing gene expression on a plasmid using recombination in vitro.
Page 106 - CALEF, 1970 Immunity phase-shift in defective lysogens: non-mutational hereditary change of early regulation of X prophage.
Page 46 - Siebenlist U., Simpson RB, and Gilbert W. 1980. E. coli RNA polymerase interacts homologously with two different promoters. Cell 20: 269-281.