A dtsR gene-disrupted mutant of Brevibacterium lactofermentum requires fatty acids for growth and efficiently produces L-glutamate in the presence of an excess of biotin

• Published in: Biochemical and biophysical research communications Vol. 234; no. 1; p. 157
• Main Authors: Kimura, E, Abe, C, Kawahara, Y, Nakamatsu, T, Tokuda, H
• Format: Journal Article
• Language: English
• Published: United States 08-05-1997
• Subjects: Bacterial Proteins - analysis; Bacterial Proteins - genetics; Bacterial Proteins - physiology; Biotin - pharmacology; Blotting, Southern; Blotting, Western; Brevibacterium - genetics; Brevibacterium - growth & development; Brevibacterium - metabolism; Detergents - pharmacology; Fatty Acids - metabolism; Genes, Bacterial; Genes, Suppressor; Glutamic Acid - biosynthesis; Mutagenesis, Site-Directed; Mutation; Oleic Acid - metabolism; Palmitic Acid - metabolism; Plasmids; Restriction Mapping
• ISSN: 0006-291X
• DOI: 10.1006/bbrc.1997.6613

A dtsR gene encoding a homolog of the beta subunit of some biotin-containing enzymes suppresses a detergent-sensitive mutation of Brevibacterium lactofermentum (E. Kimura et al., 1996, Biosci. Biotech. Biochem. 60, 1565-1570), which has been used for the fermentative production of L-glutamate. When the dtsR gene was disrupted, the organism exhibited strict fatty acid auxotrophy; oleate or oleate ester, but not palmitate ester or stearate ester, supported the growth of the delta dtsR mutant. Immunoblotting with an anti-DtsR antibody revealed that no intact DtsR was present in the cytosol of the delta dtsR mutant. In the presence of an excess of biotin, the wild type strain did not produce L-glutamate whereas the delta dtsR mutant efficiently produced it. The mechanism underlying the efficient production of L-glutamate by the delta dtsR mutant is discussed as to the possible role of dtsR in fatty acid metabolism.