Bacillus subtilis genes for the utilization of sulfur from aliphatic sulfonates

• Published in: Microbiology (Society for General Microbiology) Vol. 144; no. 9; pp. 2555 - 2561
• Main Authors: van der Ploeg, Jan R, Cummings, Nicola J, Leisinger, Thomas, Connerton, Ian F
• Format: Journal Article
• Language: English
• Published: Reading Soc General Microbiol 01.09.1998; Society for General Microbiology
• Subjects: Amino Acid Sequence; Artificial Gene Fusion; ATP-Binding Cassette Transporters - genetics; Bacillus subtilis; Bacillus subtilis - genetics; Bacillus subtilis - metabolism; Bacterial Proteins - genetics; Bacteriology; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Genes, Bacterial; Genetics; Lac Operon; Microbiology; Molecular Sequence Data; Mutagenesis, Insertional; Open Reading Frames; Operon; Sequence Homology, Amino Acid; Sulfonic Acids - metabolism; Sulfur - metabolism; Bacillales; Gene; Bacillus subtilis; Membrane transport; Bacteria; Identification; Bacillaceae; Metabolism; Sulfonate
• ISSN: 1350-0872; 1465-2080
• DOI: 10.1099/00221287-144-9-2555

Mikrobiologisches Institut, Swiss Federal Institute of Technology, ETH-Zentrum, CH-8092 Zürich, Switzerland Institute of Food Research, Department of Food Macromolecular Science, Reading Laboratory, Earley Gate, Whiteknights Road, Reading RG6 6BZ, UK ABSTRACT A 5 kb region upstream of katA at 82°G on the Bacillus subtilis chromosome contains five ORFs organized in an operon-like structure. Based on sequence similarity, three of the ORFs are likely to encode an ABC transport system (ssuBAC) and another to encode a monooxygenase (ssuD). The deduced amino acid sequence of the last ORF (ygaN) shows no similarity to any known protein. B. subtilis can utilize a range of aliphatic sulfonates such as alkanesulfonates, taurine, isethionate and sulfoacetate as a source of sulfur, but not when ssuA and ssuC are disrupted by insertion of a neomycin-resistance gene. Utilization of aliphatic sulfonates was not affected in a strain lacking 3'-phosphoadenosine 5'-phosphosulfate (PAPS) sulfotransferase, indicating that sulfate is not an intermediate in the assimilation of sulfonate-sulfur. Sulfate or cysteine prevented expression of β-galactosidase from a transcriptional ssuD::IacZ fusion. It is proposed that ssuBACD encode a system for ATP-dependent transport of alkanesulfonates and an oxygenase required for their desulfonation. * Author for correspondence: Jan R. van der Ploeg. Tel: +41 1 6323332. Fax: +41 1 6321148. Keywords: sulfonate, sulfate starvation, Bacillus subtilis, cysteine biosynthesis, ABC transporter