Structural and Functional Features of Viral Chaperonins

Chaperonins provide proper folding of proteins in vivo and in vitro and, as was thought until recently, are characteristic of prokaryotes, eukaryotes, and archaea. However, it turned out that some bacteria viruses (bacteriophages) encode their own chaperonins. This review presents results of the investigations of the first representatives of this new chaperonin group: the double-ring EL chaperonin and the single-ring OBP and AR9 chaperonins. Biochemical properties and structure of the phage chaperonins were compared within the group and with other known group I and group II chaperonins.

Automated summary

It has been discovered that some bacterial viruses also encode their own chaperonins, in addition to being characteristic of prokaryotes, eukaryotes, and archaea. The biochemical properties and structures of these new phage chaperonins have been compared with other known group I and group II chaperonins.