Uridylylation of the PII protein in Rhizobium leguminosarum.
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.
Colonna-Romano
S
S
International Institute of Genetics and Biophysics, Naples, Italy.
Patriarca
E J
EJ
Amar
M
M
Bernard
P
P
Manco
G
G
Lamberti
A
A
Iaccarino
M
M
Defez
R
R
D001345:Autoradiography; D001426:Bacterial Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005973:Glutamine / Q000378:metabolism; D007656:Ketoglutaric Acids / Q000378:metabolism; D051922:PII Nitrogen Regulatory Proteins; D011499:Protein Processing, Post-Translational; D016961:Rhizobium leguminosarum / Q000378:metabolism*; D014529:Uridine / Q000378:metabolism; D014544:Uridine Triphosphate / Q000378:metabolism*
D001426:Bacterial Proteins; D007656:Ketoglutaric Acids; D051922:PII Nitrogen Regulatory Proteins; D005973:Glutamine; C404143:PIID regulatory protein, Bacteria; D014544:Uridine Triphosphate; D014529:Uridine