| Literature DB >> 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.Entities:
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Year: 1989 PMID: 2498282 PMCID: PMC209994 DOI: 10.1128/jb.171.6.2915-2918.1989
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490