title: Uridylylation of the PII protein in Rhizobium leguminosarum.
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.
authors.affiliation: International Institute of Genetics and Biophysics, Naples, Italy.
authors.forename: S
authors.initials: S
authors.lastname: Colonna-Romano
authors.forename: E J
authors.initials: EJ
authors.lastname: Patriarca
authors.forename: M
authors.initials: M
authors.lastname: Amar
authors.forename: P
authors.initials: P
authors.lastname: Bernard
authors.forename: G
authors.initials: G
authors.lastname: Manco
authors.forename: A
authors.initials: A
authors.lastname: Lamberti
authors.forename: M
authors.initials: M
authors.lastname: Iaccarino
authors.forename: R
authors.initials: R
authors.lastname: Defez
mesh_terms: 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*
chemical_list: D001426:Bacterial Proteins; D007656:Ketoglutaric Acids; D051922:PII Nitrogen Regulatory Proteins; D005973:Glutamine; C404143:PIID regulatory protein, Bacteria; D014544:Uridine Triphosphate; D014529:Uridine