DivS, a novel SOS-inducible cell-division suppressor in Corynebacterium glutamicum

• Published in: Molecular microbiology Vol. 67; no. 3; pp. 597 - 608
• Main Authors: Ogino, Hidetaka, Teramoto, Haruhiko, Inui, Masayuki, Yukawa, Hideaki
• Format: Journal Article
• Language: English
• Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.02.2008; Blackwell Publishing Ltd; Blackwell Science
• Subjects: Anti-Bacterial Agents; Bacterial Proteins - biosynthesis; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Bacterial Proteins - physiology; Bacteriology; Biological and medical sciences; Cell Division; Corynebacterium glutamicum - cytology; Corynebacterium glutamicum - genetics; Corynebacterium glutamicum - physiology; Cytoskeletal Proteins - genetics; Cytoskeletal Proteins - metabolism; DNA Damage; Fundamental and applied biological sciences. Psychology; Gene Deletion; Gene Expression Regulation, Bacterial; Microbiology; Miscellaneous; Mitomycin - pharmacology; Rec A Recombinases - genetics; Sequence Homology, Amino Acid; SOS Response (Genetics); Cell division; Bacteria; SOS function; Actinomycetes; Corynebacteriaceae; Corynebacterium glutamicum
• ISSN: 0950-382X; 1365-2958
• DOI: 10.1111/j.1365-2958.2007.06069.x

DNA damage-induced SOS response elicits the induction of cell-division suppressor as well as DNA repair genes. In Gram-positive bacteria, cell-division suppressor genes, so far characterized from Bacillus subtilis (yneA) and Mycobacterium tuberculosis (rv2719c), share limited homology, but are both located in the vicinity of lexA on their respective genomes. Using this proximity to lexA, Corynebacterium glutamicum R divS (cgR1759) was identified as an SOS-inducible cell-division suppressor in this study. The amino acid sequence of DivS showed no homology to that of YneA and Rv2719c. divS expression was markedly induced by DNA-damaging mitomycin C treatment in wild-type cells, but not in its ΔrecA mutant cells, which are unable to induce the SOS response. Wild-type C. glutamicum R cells exposed to DNA-damaging mitomycin C exhibited elongated morphology that, using green fluorescent protein-FtsZ fusion protein, was attributed to defects in FtsZ ring assembly. Cells defective in FtsZ ring assembly were subsequently incapable of septum wall synthesis. In the presence of mitomycin C, divS mutant cells did not exhibit this elongated morphology, whereas cells overexpressing divS were elongated and abnormally branched.