URIDYLYLATION OF THE P(II) PROTEIN IN RHIZOBIUM-LEGUMINOSARUM

Permeabilization with cetyl trimethyl ammonium bromide was used to stu dy the post-translational modification of the P(II) protein in Rhizobi um leguminosarum. Upon incubation with radioactive UTP a single band w as obtained after SDS-PAGE and autoradiography. RNase resistance and s nake venom phosphodiesterase sensivity showed that radioactivity was b ound 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 glutam ine/alpha-ketoglutarate ratio.