Open AccessPhosphorylation and nucleotidylation of proteins in Rhodocyclus gelatinosus
Author(s) -
Averhoff Beate,
Antranikian Garabed,
Gottschalk Gerhard
Publication year - 1986
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1986.tb01291.x
Subject(s) - isoelectric point , biochemistry , phosphate , inosine , gel electrophoresis , biology , chemistry , protein phosphorylation , orotic acid , purine metabolism , polyacrylamide gel electrophoresis , purine , phosphorylation , microbiology and biotechnology , enzyme , protein kinase a
Cells of Rhodocyclus gelatinosus were radioactively labeled by addition of [ 32 P]orthophosphate, [ 14 C]inosine or [ 14 C]orotic acid during anaerobic growth on citrate in the light. Protein analysis by two‐dimensional gel electrophoresis and autoradiography of the gels revealed the presence of several radioactively labeled protein species in this organism. The molecular mass and the isoelectric point of all these proteins were determined. Treatment of the 32 P‐labeled protein fractions with acid and alkaline phosphatase clearly showed that at least 8 protein species were modified by phosphorylation. The experiments conducted with the 14 C‐labeled precursors of purines and pyrimidines indicated the presence of 4 protein species which were modified by a compound containing a purine and phosphate, and a single protein simultaneously being labeled with pyrimidine and phosphate.