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Structural model at atomic resolution of bacteriophage T4 [1] The structure of a typical myovirus bacteriophage Anatomy and infection cycle of bacteriophage T4.. A bacteriophage (/ b æ k ˈ t ɪər i oʊ f eɪ dʒ /), also known informally as a phage (/ ˈ f eɪ dʒ /), is a virus that infects and replicates within bacteria and archaea.
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.
M13 is one of the Ff phages (fd and f1 are others), a member of the family filamentous bacteriophage ().Ff phages are composed of circular single-stranded DNA (), which in the case of the m13 phage is 6407 nucleotides long and is encapsulated in approximately 2700 copies of the major coat protein p8, and capped with about 5 copies each of four different minor coat proteins (p3 and p6 at one ...
3. The phage DNA then moves through the cell to the host's DNA. 4. The phage DNA integrates itself into the host cell's DNA, creating prophage. 5. The prophage then remains dormant until the host cell divides. 6. After the host cell has divided, the phage DNA in the daughter cells activate, and the phage DNA begins to express itself.
A prophage is a bacteriophage (often shortened to "phage") genome that is integrated into the circular bacterial chromosome or exists as an extrachromosomal plasmid within the bacterial cell. [1] Integration of prophages into the bacterial host is the characteristic step of the lysogenic cycle of temperate phages.
Gene transfer agents, like defective prophages, arise by mutation of prophages, but they retain functional genes for the head and tail components of the phage particle (structural genes) and the genes for DNA packaging. The phage genes specifying its regulation and DNA replication have typically been deleted, and expression of the cluster of ...
T7 DNA polymerase uses E. coli's endogenous thioredoxin, a REDOX protein, as a sliding DNA clamp during phage DNA replication (though thioredoxin normally has a different function). The sliding clamp functions to hold the polymerase onto the DNA, which increases the rate of synthesis. [20]
This result was extended by inserting foreign DNA expressing a foreign peptide into fd phage gene 3, rather than into the intergenic sequence, so that the foreign peptide appears on the surface of the phage as a part of the gene 3 adsorption protein. [31] [32] [33] Phage carrying the foreign peptide can then be detected using appropriate ...