Control of Development by Altered Localization of a Transcription Factor in B. subtilis

• Published in: Molecular cell 1999-11, Vol.4 (5), p.665-672
• Main Authors: Quisel, John D, Lin, Daniel Chi-Hong, Grossman, Alan D
• Format: Article
• Language: English
• Subjects: Adenosine Triphosphatases - antagonists & inhibitors; Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - metabolism; Bacillus subtilis; Bacillus subtilis - cytology; Bacillus subtilis - genetics; Bacillus subtilis - growth & development; Bacillus subtilis - metabolism; Bacterial Proteins - antagonists & inhibitors; Bacterial Proteins - chemistry; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding Sites; Cell Polarity; Chromosomes, Bacterial - genetics; Chromosomes, Bacterial - metabolism; Conserved Sequence; DNA, Bacterial - genetics; DNA, Bacterial - metabolism; Gene Expression Regulation, Bacterial; Microscopy, Fluorescence; Mutation - genetics; ParA protein; ParB protein; Promoter Regions, Genetic - genetics; Recombinant Fusion Proteins - metabolism; Sigma Factor; Soj protein; Spo0J protein; Spores, Bacterial - cytology; Spores, Bacterial - genetics; Spores, Bacterial - growth & development; Spores, Bacterial - metabolism; Transcription Factors - antagonists & inhibitors; Transcription Factors - chemistry; Transcription Factors - genetics; Transcription Factors - metabolism
• ISSN: 1097-2765; 1097-4164
• DOI: 10.1016/S1097-2765(00)80377-9

In B. subtilis, the chromosome partitioning proteins Soj (ParA) and Spo0J (ParB) regulate the initiation of sporulation. Soj is a negative regulator of sporulation gene expression, and Spo0J antagonizes Soj function. Using fusions of Soj to green fluorescent protein, we found that Soj localized near the cell poles and upon entry into stationary phase oscillated from pole to pole. In the absence of Spo0J, Soj was associated predominantly with DNA. By in vivo cross-linking and immunoprecipitation, we found that Soj physically associates with developmentally regulated promoters, and this association increased in the absence of Spo0J. These results show that Soj switches localization and function depending on the chromosome partitioning protein Spo0J. We further show that mutations in the Soj ATPase domain disrupt localization and function and render Soj insensitive to regulation by Spo0J.