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Lambda phage is a non-contractile tailed phage, meaning during an infection event it cannot 'force' its DNA through a bacterial cell membrane. It must instead use an existing pathway to invade the host cell, having evolved the tip of its tail to interact with a specific pore to allow entry of its DNA to the hosts.
[4] cII acts as a transcriptional activator of three promoters on the phage genome: pI, pRE, and pAQ. [3] cII is an unstable protein with a half-life as short as 1.5 mins at 37˚C, [5] enabling rapid fluctuations in its concentration. First isolated in 1982, [6] cII's function in lambda's regulatory network has been extensively studied.
Antitermination in lambda is induced by two quite distinct mechanisms. The first is the result of interaction between lambda N protein and its targets in the early phage transcripts, and the second is the result of an interaction between the lambda Q protein and its target in the late phage promoter. We describe the N mechanism first.
In molecular biology, the Cro repressor family is a family of repressor proteins in bacteriophage lambda that includes the Cro repressor. Bacteriophage lambda encodes two repressors: the Cro repressor that acts to turn off early gene transcription during the lytic cycle , and the lambda or cI repressor required to maintain lysogenic growth.
HU and integration host factor function as auxiliary proteins in cleavage of phage lambda cohesive ends by terminase is an academic journal written by the Department of Molecular Genetics. In their article, they created isogenic strains of E.coli that were lacking HU or integration host factors to test whether bacteriophage would grow under ...
Recombination between two DNA sites begins by the recognition and binding of these sites – one site on each of two separate double-stranded DNA molecules, or at least two distant segments of the same molecule – by the recombinase enzyme. This is followed by synapsis, i.e. bringing the sites together to form the synaptic complex.
The helix-turn-helix motif is a DNA-binding motif. The recognition and binding to DNA by helix-turn-helix proteins is done by the two α helices, one occupying the N-terminal end of the motif, the other at the C-terminus. In most cases, such as in the Cro repressor, the second helix contributes most to DNA recognition, and hence it is often ...
Lambda holin S (Lysis protein S of phage lambda, holin S105; TC# 1.E.2.1.1) is the prototype for class I holins. It has 3 TMSs with the N-terminus in the periplasm and the C-terminus in the cytoplasm. Its 107 codon sequence encodes two proteins with opposing functions, the holin, S105, and the holin inhibitor, S107.