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Permeabilization with cetyl trimethyl ammonium bromide was used to study the post-translational modification of the P II protein in Rhizobium leguminosarum. Upon incubation with radioactive UTP a single band was obtained after SDS-PAGE and autoradiography. RNase resistance and snake venom phosphodiesterase sensivity showed that radioactivity was bound through a phosphodiester bond to a protein which was absorbed by an antiserum specific for the P II protein. Uridylylation of the P II protein was shown to be dependent on the modifications of the glutamine/α-ketoglutarate ratio.