Development of Efficient Genome-Reduction Tool Based on Cre/ System in .

has been extensively studied for its excellent ability to degrade artificial chemicals and its capability to synthesize biosurfactants and antibiotics. In recent years, studies have attempted to use as a gene expression host. Various genetic tools, such as plasmid vectors, transposon mutagenesis, and gene disruption methods have been developed for use in ; however, no effective method has been reported for performing large-size genome reduction.

Complete Genome Sequence of Rhodococcus erythropolis JCM 2895, an Antibiotic Protein-Producing Strain.

The complete genome sequence of Rhodococcus erythropolis JCM 2895, an antibiotic protein-producing strain, was determined. It consists of a 6,455,263-bp chromosome, one linear plasmid (pR09L01 [227,989 bp]), and three circular plasmids (pR09C01 [79,600 bp], pREC01 [5,420 bp], and pREC02 [5,444 bp]).

Identification of a novel bacteriocin-like protein and structural gene from Rhodococcus erythropolis JCM 2895, using suppression-subtractive hybridization.

A novel bacteriocin-like protein and its structural gene (rap) were identified from Rhodococcus erythropolis JCM 2895. The rapA and B genes are located on a 5.4-kb circular plasmid, and were obtained using a modified suppression-subtractive hybridization method.

Draft Genome Sequence of Rhodococcus erythropolis JCM 6824, an Aurachin RE Antibiotic Producer.

Rhodococcus erythropolis JCM 6824 is the producer of the quinoline antibiotic aurachin RE. This bacterium also degrades and utilizes some aromatic compounds, such as biphenyl and benzoate. Here, we report the draft genome sequence of this strain.

Structure of the quinoline N-hydroxylating cytochrome P450 RauA, an essential enzyme that confers antibiotic activity on aurachin alkaloids.

The cytochrome P450 RauA from Rhodococcus erythropolis JCM 6824 catalyzes the hydroxylation of a nitrogen atom in the quinolone ring of aurachin, thereby conferring strong antibiotic activity on the aurachin alkaloid. Here, we report the crystal structure of RauA in complex with its substrate, a biosynthetic intermediate of aurachin RE. Clear electron density showed that the quinolone ring is oriented parallel to the porphyrin plane of the heme cofactor, while the farnesyl chain curls into a U-shape topology and is buried inside the solvent-inaccessible hydrophobic interior of RauA.

Cloning and heterologous expression of the aurachin RE biosynthesis gene cluster afford a new cytochrome P450 for quinoline N-hydroxylation.

Aurachin RE is a prenylated quinoline antibiotic that was first isolated from the genus Rhodococcus. It shows potent antibacterial activity against a variety of Gram-positive bacteria. Here we have identified a minimal biosynthesis gene cluster for aurachin RE in Rhodococcus erythropolis JCM 6824 by using random transposon mutagenesis and heterologous production.