Project name: Corynebacterium glutamicum ATCC 13032

Description: Active segregation of DNA in bacteria is catalyzed by cytomotive structures. Mediators of subcellular plasmid positioning are Walker-type ATPases (ParA), actin-like proteins, or tubulin homologs. These motor proteins are coupled to the DNA via adaptor proteins that recognize specific DNA motifs. Here, we describe that a temperate phage, CGP3, integrated into the genome of Corynebacterium glutamicum ATCC 13032 encodes an actin-like protein, AlpC. Biochemical characterization confirms that AlpC is a bona fide actin-like protein and cell biological analysis shows that AlpC forms dynamic filamentous structures upon phage induction. The co-transcribed AlpA protein binds to a specific region of the phage DNA, possibly functioning as an adaptor protein that connects circular phage DNA to the tips of the AlpC filaments. The AlpC filaments transport phage DNA to the cell membrane of the host cell. Furthermore, both AlpA and AlpC are required for efficient phage replication. This is remarkably similar to actin-assisted membrane localization of eukaryotic viruses that use the actin cytoskeleton to concentrate virus particles at the egress sites.Overall design: To identify the stress response induced by the antibiotic agent mitomycin C, DNA microarray analyses were performed of ATCC 13032 wild type cells treated with 0.6 mM mitomycin C in comparison to untreated cells at one, three, and six hours after addition of mitomycin C. For this purpose RNA was isolated from cells cultivated in CGXII minimal medium with 4% glucose, either treated with 0.6 µM Mitomycin C or untreated. Mitomycin C was added at an OD of 3 and cells were harvested after one, three, and six hours after addition of mitomycinC. Three biological replicates were performed for each time point.

Data type: Transcriptome or Gene expression

Sample scope: Multiisolate

Relevance: Industrial

Last updated: 2013-04-09