Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis.
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.
Mitchell
C
C
Department of Biochemistry, University of Illinois, Chicago 60612.
Morris
P W
PW
Vary
J C
JC
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000737:chemistry / Q000502:physiology*; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism*; D013171:Spores, Bacterial
D001426:Bacterial Proteins; D010750:Phosphoproteins; D000255:Adenosine Triphosphate