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Increased phosphorylation of a ribosomal protein during aggregation of the slime mold Dictyostelium discoideum
Author(s) -
Juliani Maria Helena,
José Carlos da Costa Maia,
Maria Christina Manhães Bonato
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80191-4
Subject(s) - dictyostelium discoideum , slime mold , ribosomal protein , phosphorylation , protein phosphorylation , biochemistry , chemistry , microbiology and biotechnology , ribosomal rna , ribosomal protein s6 , polyacrylamide gel electrophoresis , dictyostelium , biology , ribosome , rna , protein kinase a , enzyme , gene
A single ribosomal protein ( M r 32 000) becomes phosphorylated during differentiation of Dictyostelium discoideum amoebae. This protein is tentatively identified as the 40 S ribosomal protein S 6 . Phosphorylation of S 6 is monitored by incorporation of 32 P i and by two‐dimensional polyacrylamide gel electrophoresis. S 6 is minimally phosphorylated in growing cells. Upon starvation, S 6 is progressively phosphorylated, the degree of phosphorylation being maximal during the aggregation phase of the developmental cycle.