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Enterobacteria phage λ (lambda phage, coliphage λ, officially Escherichia virus Lambda) is a bacterial virus, or bacteriophage, that infects the bacterial species Escherichia coli (E. coli). It was discovered by Esther Lederberg in 1950. [ 2 ]
In microbiology, the multiplicity of infection or MOI is the ratio of agents (e.g. phage or more generally virus, bacteria) to infection targets (e.g. cell).For example, when referring to a group of cells inoculated with virus particles, the MOI is the ratio of the number of virus particles to the number of target cells present in a defined space.
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. Together the Cro and cI repressors form a helix-turn-helix (HTH) superfamily. The lambda Cro repressor binds to DNA as a highly flexible dimer.
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After Benzer demonstrated the power of the T4 rII system for exploring the fine structure of the gene, others adapted the system to explore related problems.For example, Francis Crick and others used one of the peculiar r mutants Benzer had found (a deletion that fused the A and B cistrons of rII) to demonstrate the triplet nature of the genetic code.
The discovery of the helix-turn-helix motif was based on similarities between several genes encoding transcription regulatory proteins from bacteriophage lambda and Escherichia coli: Cro, CAP, and λ repressor, which were found to share a common 20–25 amino acid sequence that facilitates DNA recognition. [2] [3] [4] [5]
From Wikipedia, the free encyclopedia. Redirect page. Redirect to: Lambda phage
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.