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Uridylylation of the PII protein in Rhizobium leguminosarum
S Colonna-Romano1, E J Patriarca, M Amar
1International Institute of Genetics and Biophysics, Naples, Italy.
FEBS Letters
|September 6, 1993
Abstract:
Permeabilization with cetyl trimethyl ammonium bromide was used to study the post-translational modification of the PII 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 sensitivity showed that radioactivity was bound through a phosphodiester bond to a protein which was absorbed by an antiserum specific for the PII protein. Uridylylation of the PII protein was shown to be dependent on the modifications of the glutamine/alpha-ketoglutarate ratio.