Proteins that interact with GTP during sporulation of Bacillus subtilis.
During sporulation of Bacillus subtilis, several proteins were shown to interact with GTP in specific ways. UV light was used to cross-link [alpha-32P]GTP to proteins in cell extracts at different stages of growth. After electrophoresis, 11 bands of radioactivity were found in vegetative cells, 4 more appeared during sporulation, and only 9 remained in mature spores. Based on the labeling pattern with or without UV light to cross-link either [alpha-32P]GTP or [gamma-32P]GTP, 11 bands of radioactivity were apparent guanine nucleotide-binding proteins, and 5 bands appeared to be phosphorylated and/or guanylated. Similar results were found with Bacillus megaterium. Assuming that GTP might be a type of signal for sporulation, it could interact with and regulate proteins by at least three mechanisms.
Mitchell
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Department of Biochemistry, University of Illinois, Chicago 60612.
Vary
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JC
D001412:Bacillus subtilis / Q000502:physiology*; D001426:Bacterial Proteins / Q000502:physiology; D019204:GTP-Binding Proteins / Q000502:physiology*; D006160:Guanosine Triphosphate / Q000502:physiology*; D008970:Molecular Weight; D010766:Phosphorylation; D013172:Spores, Fungal
D001426:Bacterial Proteins; D006160:Guanosine Triphosphate; D019204:GTP-Binding Proteins