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Lambda phage J protein interaction with the LamB porin 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 ...
[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.
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.
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.
Several attempts have been made to map protein–protein interactions among phage and their host. For instance, bacteriophage lambda was found to interact with its host, E. coli, by dozens of interactions. Again, the significance of many of these interactions remains unclear, but these studies suggest that there most likely are several key ...
a Bacteriophage lambda outer membrane protein, Lom [6] OspA/B are lipoproteins from Borrelia burgdorferi. OspA and OspB share 53% amino acid identity and likely have a similar antiparallel “free-standing” β sheet protein structure associated with the outer membrane surface via a lipidated NH2-terminal cysteine residue. [7] OspA
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 ...
In order to solve such a problem, phage viruses synthesize another protein called holin which binds to the cell membrane and makes holes in it (hence its name), allowing lysins to reach the peptidoglycan matrix. The prototypical holin is the lambda phage S protein, which assists the lambda phage R protein (lysin).