The tail of a chaperonin: the C‐terminal region of Esctierichia coli GroEL protein

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Abstract
The active form of the HSP60 molecular chaperone of Escherichia coli, GroEL, is a pair of seven-membered rings. We have used site-directed mutagenesis to construct forms of the 547-amino-acid monomer truncated at the C-terminus. We show here that forms that are 520 amino acids long or longer are close to being fully functional. Removing one further amino acid, however, results in a protein, GroEL519, which retains little function. This truncated form is metabolically stable but is not recovered from the cell in particle form. When synthesized at high levels, it prevents the normal assembly of GroEL547 present in the same cell. When synthesized at low levels, it can be included, probably at low molar ratios, in particles formed by assembly-competent forms of GroEL. This can be seen as partial complementation of the temperature-sensitive mutant groEL44. We conclude that amino acid 520 is crucial for particle assembly. GroEL516 has in vivo properties similar to those of GroEL516 has in vivo properties similar to those of GroEL519, but the still shorter form, GroEL504, appears to be inactive.