Open AccessIdentification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis
Author(s) -
C. A. Mitchell,
Paul W. Morris,
James C. Vary
Publication year - 1992
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.174.8.2474-2477.1992
Subject(s) - bacillus subtilis , biology , biochemistry , phosphorylation , in vitro , homology (biology) , elongation factor , gel electrophoresis , membrane protein , peptide sequence , microbiology and biotechnology , amino acid , bacteria , gene , membrane , rna , genetics , ribosome
Protein phosphorylation in Bacillus subtilis was assayed in vitro by using extracts prepared from cells at various times during growth and sporulation. At least six proteins were labeled in vitro by using [gamma-32P]ATP and extracts of vegetative cells. In extracts prepared at the end of exponential growth and during stationary phase, 12 to 13 proteins were labeled. Seven of the phosphoproteins were purified by fast-performance liquid chromatography and polyacrylamide gel electrophoresis, blotted to Immobilon membranes, and subjected to partial protein sequencing. One of the sequences had sequence homology (greater than 45%) to elongation factor G from several bacterial species, and four sequences matched the predicted amino-terminal sequences of the outB, orfY-tsr, orfU, and ptsH genes.