Chaperones in bacteriophage T4 assembly.

Protein folding in the cell is controlled at the levels of translation and post-translational modification, depends on a number of conserved proteins known as chaperones, and is catalyzed by specific enzymes, such as protein disulfide isomerase and peptidyl prolyl cis-trans isomerase. The chaperones stabilize folding intermediates and participate in assembly and disaggregation of supramolecular structures. Bacteriophage T4 is an especially convenient system for studying of protein folding mechanisms, since its genome encodes several virus-specific chaperones. In this review, the chaperones of phage T4 that take part in capsid formation (gp31 and gp40) and in folding and assembly of virion tail fibers (gp38, gp57A) have been considered. Protein encoded by gene 31 completely substitutes co-chaperonin GroES of the host cell in folding of the major capsid protein, gp23, aided by chaperonin GroEL. The product of gene 40, which is homologous to analogs of eukaryotic GroEL and peptidyl prolyl cis-trans isomerase, participates in assembly of gp20 while the formation of procapsid connector. The chaperone encoded by gene 57A is essential for folding and oligomerization of both long and short phage tail fibers. gp38, together with gp57A, participates in the formation of the distal part of the long fibers. This protein seems to represent a principally new group of chaperones that change steric structure of folded polypeptide. One phage chaperone, fibritin, encoded by gene wac (whiskers antigen control) and taking part in assembly the subunits of the long tail fibers is a constituent of the virion. Fibritin is a convenient model for studying mechanisms of folding and oligomerization of fibrous proteins due to its labile triple-stranded alpha-helical coiled-coil structure.