Sm. Vandervies et al., BACTERIOPHAGE-T4 ENCODES A CO-CHAPERONIN THAT CAN SUBSTITUTE FOR ESCHERICHIA-COLI GROES IN PROTEIN-FOLDING, Nature, 368(6472), 1994, pp. 654-656
SEVERAL bacteriophages use the Escherichia coli GroES and GroEL chaper
onins for folding and assembly of their morphogenetic structures1. Bac
teriophage T4 is unusual in that it encodes a specialized protein (Gp3
1) that is thought to interact with the host GroEL and to be absolutel
y required for the correct assembly of the major capsid protein (Gp23)
in vivo2-4. Here we show that despite the absence of amino-acid seque
nce similarity between Gp31 and GroES5,6 Gp31 can functionally substit
ute for the GroES co-chaperonin in the morphogenesis of bacteriophages
lambda and T5, the in vivo and in vitro chaperonin-dependent assembly
of ribulose bisphosphate carboxylase (Rubisco), as well as overall ba
cterial growth at the non-permissive temperature. Like GroES, the bact
eriophage Gp31 protein forms a stable complex with the E. coli GroEL p
rotein in the presence of Mg-ATP and inhibits the ATPase activity of G
roEL in vitro.