Editing Bacteriocin (section)

====Tailocins====
Most well studied are the tailocins of ''[[Pseudomonas aeruginosa]]''. They can be further subdivided into R-type and F-type pyocins.<ref>{{cite journal | vauthors = Ghequire MG, De Mot R | title = Ribosomally encoded antibacterial proteins and peptides from Pseudomonas | journal = FEMS Microbiology Reviews | volume = 38 | issue = 4 | pages = 523–68 | date = July 2014 | pmid = 24923764 | doi = 10.1111/1574-6976.12079 | doi-access = free }}</ref>
Some research was made to identify the pyocins and show how they are involved in the “cell-to-cell” competition of the closely related Pseudomonas bacteria.

The two types of tailocins differ by their structure; they are both composed of a sheath and a hollow tube forming a long helicoidal hexameric structure attached to a baseplate. There are multiple tail fibers that allow the viral particle to bind to the target cell. However, the R-pyocins are a large, rigid contractile tail-like structure whereas the F-pyocins are a small flexible, non-contractile tail-like structure.

The tailocins are coded by prophage sequences in the bacteria genome, and the production will happen when kin bacteria are spotted in the environment of the producer. 
The particles are synthesized in the center of the cells and after maturation they will migrate to the cell pole via tubulin structure. The tailocins will then be ejected in the medium with the cell lysis. They can be projected up to several tens of micrometers thanks to a very high turgor pressure of the cell. The tailocins released will then recognize and bind to the kin bacteria to kill them.<ref>{{cite journal | vauthors = Vacheron J, Heiman CM, Keel C| title = Live cell dynamics of production, explosive release and killing activity of phage tail-like weapons for Pseudomonas kin exclusion | journal = Communications Biology | volume = 87 | issue = 4 | date = January 2021 | page = 87 | doi =10.1038/s42003-020-01581-1 | pmid = 33469108 | pmc = 7815802 }}</ref>