PURIFICATION AND PROPERTIES OF GROE, A HOST PROTEIN INVOLVED IN BACTERIOPHAGE ASSEMBLY

A method is presented for the purification of gp groE, an Escherichia coli protein which is required for correct assembly of bacteriophages λ, T4, T5 and others, gp groE is a soluble protein which is found as an oligomer containing 14 subunits of molecular weight 65,000 each. The gp groE particle is cylindrical with a diameter of 125 Å and a height of 100 Å, and it has 7-fold rotational symmetry. It has a weak ATPase activity, and is identical to a protein commonly found to copurify with RNA polymerase and which was originally misidentified as RNA polymerase. © 1979.