Orf5/SolR: a transcriptional repressor of the sol operon of Clostridium acetobutylicum?

• Published in: Journal of industrial microbiology & biotechnology 2001-11, Vol.27 (5), p.307-313
• Main Authors: Thormann, K, Dürre, P
• Format: Article
• Language: English
• Subjects: Acetone - metabolism; Alcohol Dehydrogenase - genetics; Aldehyde Oxidoreductases - genetics; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Binding sites; Biotechnology; Butanols - metabolism; Cloning, Molecular; Clostridium - genetics; Clostridium acetobutylicum; Coenzyme A-Transferases; Deoxyribonucleic acid; DNA; DNA-Binding Proteins - genetics; DNA-Binding Proteins - metabolism; E coli; Enzymes; Escherichia coli - genetics; Escherichia coli Proteins; Gene Expression Regulation, Bacterial; Genes; Genes, Bacterial; Genetic engineering; Microbiology; Multienzyme Complexes - genetics; Operon - genetics; Orf5 gene; Plasmids; Proteins; Repressor Proteins - genetics; Repressor Proteins - metabolism; Solvents; Solvents - metabolism; Studies
• ISSN: 1367-5435; 1476-5535
• DOI: 10.1038/sj.jim.7000144

The gene of Orf5 (SolR) of Clostridium acetobutylicum DSM 792 was subcloned and overexpressed in Escherichia coli. The protein was purified with Ni-NTA agarose and used for DNA binding assays. No DNA binding of Orf5 to regions upstream of the sol operon from C. acetobutylicum was observed. Overexpression of Orf5 in C. acetobutylicum led to a change in the organism's pattern of glycosylated exoproteins. The Orf5 protein was localized in the cell membrane fraction and to a small extent in the supernatant medium. Based on these results Orf5 (SolR) appears not to act as a transcriptional repressor in C. acetobutylicum, but instead may be an enzyme involved in glycosylation or deglycosylation.