Vibrio holin family

The Vibrio Holin Family (TC# 1.E.30) consists of small proteins 50 to 65 amino acyl residues in length that exhibit a single N-terminal transmembrane domain. A representative list of proteins belonging to the Vibrio Holin family can be found in the Transporter Classification Database.[1]

One member of this family is part of the lysis system of the lipid-containing double-stranded DNA bacteriophage PM2 infecting Gram-negative marine Pseudoalteromonas species (Gp-K; TC# 1.E.30.1.1).[2] Phage PM2 uses a novel system to disrupt the infected cell. The Gp-K protein is needed for the permeabilization of the cytoplasmic membrane and appears to play the role of a typical holin. It has 53 aas and 1 transmembrane domain (TMS). Unlike other bacteriophages studied, PM2 relies on lytic factors of a cellular origin for digestion of the peptidoglycan. Another protein, Gp-l (51 aa, no TMDs), is needed for disruption of the outer membrane, which is highly rigidified by the divalent cations abundant in the marine environment. Gp-l has no precedent in other phage lytic systems studied so far, but is present in genomes of other bacterial viruses suggesting that the same system might be used by other phages and is not unique to PM2.[1][2]

See also

References

  1. 1 2 "1.E.30 The Vibrio Holin (Vibrio Holin) Family". Transporter Classification Database. Retrieved 2016-03-28.
  2. 1 2 Krupovic, Mart; Daugelavicius, Rimantas; Bamford, Dennis H. (2007-06-01). "A novel lysis system in PM2, a lipid-containing marine double-stranded DNA bacteriophage". Molecular Microbiology. 64 (6): 1635–1648. doi:10.1111/j.1365-2958.2007.05769.x. ISSN 0950-382X. PMID 17555443.

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