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T4 is capable of undergoing only a lytic life cycle and not the lysogenic life cycle. The species was formerly named T-even bacteriophage, a name which also encompasses, among other strains (or isolates), Enterobacteria phage T2, Enterobacteria phage T4 and Enterobacteria phage T6.
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.
The T4 rII system is an experimental system developed in the 1950s by Seymour Benzer for studying the substructure of the gene. The experimental system is based on genetic crosses of different mutant strains of bacteriophage T4, a virus that infects the bacteria Escherichia coli.
However, some tailed bacteriophage genomes can vary quite significantly in nucleotide sequence, even among the same genus. Due to their characteristic structure and possession of potentially homologous genes, it is believed these bacteriophages possess a common origin.
Bacteriophage T4 is a particularly well studied virus and its protein quaternary structure is relatively well defined. [10] A study by Floor (1970) [ 11 ] showed that, during the in vivo construction of the virus by specific morphogenetic proteins, these proteins need to be produced in balanced proportions for proper assembly of the virus to occur.
During assembly of the bacteriophage (phage) T4 virion, the structural proteins encoded by the phage genes interact with each other in a characteristic sequence. Maintaining an appropriate balance in the amounts of each of these structural proteins produced during viral infection appears to be critical for normal phage T4 morphogenesis. [4]
LIN involves the antiholin rI protein of T4 (See TC# 1.E.8.1.1). [5] Lysis inhibition is an effective strategy to coordinate lysis timing with phage particle maturation and to exclude other phage. [6] The C-terminal periplasmic domain of T4 holin binds the periplasmic domain of T4 antiholin (RI; 97 aas) which like the holin, spans the membrane ...
The bacterium E. coli is the host for bacteriophage T4 that has a prolate head structure. The bacteriophage encoded gp31 protein appears to be functionally homologous to E. coli chaperone protein GroES and able to substitute for it in the assembly of bacteriophage T4 virions during infection. [21]