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J. Biol. Chem., Vol. 269, Issue 45, 27941-27951, Nov, 1994
CL Gordon, SK Sather, S Casjens and J King
The in vivo conformational substrates of the GroE chaperonins have been
difficult to identify, in part because of limited information on in vivo
polypeptide chain folding pathways. Temperature-sensitive folding (tsf)
mutants have been characterized for the coat protein and tailspike protein
of phage P22. These mutations block intracellular folding at restrictive
temperature by increasing the lability of folding intermediates without
impairing the stability or function of the native state. Overexpression of
GroEL/ES suppressed the defects of tsf mutants at 17 sites in the coat
protein, by improving folding efficiency rather than assembly efficiency or
protein stability. Immunoprecipitation experiments demonstrated that GroEL
interacted transiently with newly synthesized wild-type coat protein and
that this interaction was prolonged by the tsf mutations. Folding defects
of the tailspike polypeptide chains were not suppressed. A fraction of the
tsf mutant tailspike chains bound to GroEL but were inefficiently
discharged. The results suggest that 1) thermolabile folding intermediates
are natural substrates of GroEL/ES; 2) although GroEL may bind such
intermediates for many proteins, the chaperoning function is limited to a
subset of substrate proteins; and 3) a key reason for the heat-shock
response may be to stabilize thermolabile folding intermediates at elevated
temperatures.
Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
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