PMID: 8987652Oct 1, 1996Paper

Molecular cloning of a novel gene, dtsR, which rescues the detergent sensitivity of a mutant derived from Brevibacterium lactofermentum

Bioscience, Biotechnology, and Biochemistry
E KimuraT Nakamatsu

Abstract

Several strains of Corynebacterium and Brevibacterium are known for their ability to secrete large amounts of amino acids, especially L-glutamate. We focused on the mechanism of L-glutamate secretion triggered by a detergent, namely polyoxyethylenesorbitan monopalmitate (PESP). A mutant strain, AJ11060, derived from Brevibacterium lactofermentum ATCC 13869 indicates the sensitivity to PESP. A multicopy suppresser gene that compliments the sensitivity of AJ11060 to the detergent was derived from a gene library of B. lactofermentum AJ12036. A 2855-bp DNA fragment was cloned and sequenced. An open reading frame was found that coded for the rescuer gene of the sensitivity to PESP of AJ11060 and was designated dtsR. The expression of the dtsR gene in B. lactofermentum was confirmed by using anti-DtsR antibody. The deduced DtsR protein indicated significant homology with some biotin enzymes such as the beta chain of propionyl-CoA carboxylase from rat (48.3%) and human (48.7%), or a 12S chain of methylmalonyl-CoA carboxyltransferase from Propionibacterium freudenreichii (43.1%).

Citations

Apr 25, 2001·Applied and Environmental Microbiology·A LoosA J Sinskey
Dec 13, 2006·Applied and Environmental Microbiology·Yoko AsakuraTsuyoshi Nakamatsu
Feb 6, 2007·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Minoru YamadaToshiya Senda
Feb 26, 2008·Journal of Bioscience and Bioengineering·Takuo HasegawaTsuyoshi Nakamatsu
May 28, 2004·Molecular Biology and Evolution·Yousuke NishioKazuho Ikeo
Jun 8, 2018·Applied Microbiology and Biotechnology·Qiongqiong ZhangYanhe Ma
Feb 23, 2020·Journal of Agricultural and Food Chemistry·Jaeseung HongMin-Kyu Oh

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