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J. Biol. Chem., Vol. 261, Issue 26, 12414-12419, 09, 1986
GN Chandrasekhar, K Tilly, C Woolford, R Hendrix and C Georgopoulos
The morphogenesis of lambda proheads is governed by the products of at
least four bacteriophage-coded genes (B, C, E and Nu3) and two host- coded
genes (groES (mopB) and groEL (mopA)). Earlier genetic experiments
indicated that the phenotypes of some of the groES- mutations could be
suppressed by mutations in the groEL gene, suggesting an interaction
between the two groE proteins in vivo (Tilly, K., and Georgopoulos, C. P.
(1982) J. Bacteriol. 149, 1082-1088). The Mr 15,000 groES protein was
overproduced and purified to homogeneity by monitoring its presence after
polyacrylamide gel electrophoresis. Both gel filtration on an AcA34 sizing
column and glycerol gradient centrifugation indicate that the groES protein
possesses an oligomeric structure of Mr 80,000. In agreement, electron
microscopic pictures of the purified groES protein show that it possesses a
symmetrical ring- like structure. The sequence of the first five amino
acids and the overall composition of the purified protein match those
predicted by the nucleotide sequence of the groES gene. The following
results implicate a physical association between the groES and groEL
proteins in vitro. The groES protein inhibits the weak ATPase activity of
the groEL protein, with a maximal effect seen at a 1:1 molar ratio; the two
proteins cosediment during glycerol gradient centrifugation in the presence
of ATP and Mg2+; and the groES protein binds specifically to a
groEL-affinity column. These results help explain why mutations in either
of the groE genes exhibit similar phenotypes with respect to both lambda
and bacterial growth.
Purification and properties of the groES morphogenetic protein of Escherichia coli
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