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. 1989 Jun;171(6):2915–2918. doi: 10.1128/jb.171.6.2915-2918.1989

Proteins that interact with GTP during sporulation of Bacillus subtilis.

C Mitchell 1, J C Vary 1
PMCID: PMC209994  PMID: 2498282

Abstract

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.

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Selected References

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