Abstract
SEVERAL bacteriophages use the Escherichia coli GroES and GroEL chaperonins for folding and assembly of their morpho-genetic structures1. Bacteriophage T4 is unusual in that it encodes a specialized protein (Gp31) that is thought to interact with the host GroEL and to be absolutely required for the correct assembly of the major capsid protein (Gp23) in vivo2–4. Here we show that despite the absence of amino-acid sequence similarity between Gp31 and GroES5,6, Gp31 can functionally substitute for the GroES co-chaperonin in the morphogenesis of bacteriophages Λ and T5, the in vivo and in vitro chaperonin-dependent assembly of ribulose bisphosphate carboxylase (Rubisco), as well as overall bacterial growth at the non-permissive temperature. Like GroES, the bacteriophage Gp31 protein forms a stable complex with the E. coli GroEL protein in the presence of Mg-ATP and inhibits the ATPase activity of GroEL in vitro
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van der Vies, S., Gatenby, A. & Georgopoulos, C. Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein folding. Nature 368, 654–656 (1994). https://doi.org/10.1038/368654a0
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DOI: https://doi.org/10.1038/368654a0
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