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Moore M,
Svenson C,
Bowling D,
Glenn D,
( 2003 ) Complete nucleotide sequence of a native plasmid from Brevibacterium linens. PMID : 12726769 : Abstract >>
Brevibacterium linens has commercial significance in the dairy industry and potential application in the production of bacteriocins and carotenoids. Strain development of these industrially significant organisms would be facilitated by the use of vectors, yet few are available. In this study we report the isolation of four novel plasmids from the Gram-positive coryneform B. linens, and determine the first complete nucleotide sequence of a native plasmid of B. linens. The cryptic plasmid pLIM is 7610 bp in length, and belongs to a subfamily of theta replicating ColE2-related plasmids. Initial investigation suggests that replication in pLIM requires two replicases, a primase (RepA) and a DNA binding protein (RepB), encoded by a single operon repAB. The origin of replication is located upstream of repAB transcription.
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2. |
Krubasik P,
( 2000 ) A carotenogenic gene cluster from Brevibacterium linens with novel lycopene cyclase genes involved in the synthesis of aromatic carotenoids. PMID : 10821176 : DOI : 10.1007/s004380051186 Abstract >>
The carotenogenic (crt) gene cluster from Brevibacterium linens, a member of the commercially important group of coryneform bacteria, was cloned and identified. An expression library of B. linens genes was constructed and a fragment of the crt cluster was obtained by functional complementation of a colourless B. flavum mutant, screening transformed cells for production of a yellow pigment. Subsequent screening of a cosmid library resulted in the cloning of the whole crt cluster from B. linens. All genes necessary for the synthesis of the aromatic carotenoid isorenieratene were identified on the basis of sequence homologies. In addition a novel type of lycopene cyclase was identified by complementation of a lycopene-accumulating B. flavum mutant. Two genes, named crt Yc and crt Yd, which code for polypeptides of 125 and 107 amino acids, respectively, are necessary to convert lycopene to beta-carotene. The amino acid sequences of these polypeptides show no similarity to any of the known lycopene cyclases. This is the first example of a carotenoid biosynthetic conversion in which two different gene products are involved, probably forming a heterodimer.
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3. |
Yanase H,
Mitsui R,
Yurimoto H,
Fukasaka S,
Ishikawa J,
( 1999 ) A new carboxylesterase from Brevibacterium linens IFO 12171 responsible for the conversion of 1,4-butanediol diacrylate to 4-hydroxybutyl acrylate: purification, characterization, gene cloning, and gene expression in Escherichia coli. PMID : 10361681 : DOI : 10.1271/bbb.63.688 Abstract >>
A carboxylesterase that is responsible for conversion of 1,4-butanediol diacrylate (BDA) to 4-hydroxybutyl acrylate (4HBA) was found in Brevibacterium lines IFO 12171, and purified to homogeneity. The purified enzyme was active toward a variety of diesters of ethylene glycol, 1,4-butanediol, and 1,6-hexanediol. The K(m) and kcat of the enzyme for BDA were 3.04 mM and 203,000 s-1, respectively. The reaction with the purified enzyme gave 98 mM 4HBA from 100 mM BDA for 60 min. The enzyme gene was cloned from the chromosomal DNA of the bacterium. The open reading frame encoding the enzyme was 1176 bp long, corresponding to a protein of 393 amino acid residues (molecular mass = 42,569 Da). The deduced amino acid sequence contained the tetra peptide motif sequence, STTK, and the serine residue was confirmed to be the catalytic center of BDA esterase by site-directed mutagenesis for several amino acid residues. The gene was expressed in Escherichia coli under the control of the lac promoter, and the gene product (a fusion protein with 6 amino acid residues from beta-galactosidase) showed the same catalytic properties as the enzyme from the parent strain.
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4. |
Simonet JM,
( 1999 ) A gene (tmpA) for an efflux protein of the transporter family III from Brevibacterium linens OC2, an antibacterial substance-producing strain. PMID : 10341071 : Abstract >>
A gene (tmpA) encoding a putative transmembrane protein has been cloned from B. linens OC2, an antibacterial substance-producing strain. The deduced TmpA protein sequence shares similarities to members of the transporter family III exploiting the transmembrane proton gradient to provide export of toxic compounds such as antiseptics or antibiotics. Northern blot analysis indicated that tmpA gene is expressed. Length of RNA messenger and overlapping of ORFs upstream tmpA gene suggested that it might belong to an operon. The tmpA gene is unusual among B. linens species since it was not detected among eight B. linens collection strains and 40 B. linens industrial strains.
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5. |
Schroeckh V,
Martin K,
( N/A ) Resuscitation-promoting factors: distribution among actinobacteria, synthesis during life-cycle and biological activity. PMID : 16779632 : DOI : 10.1007/s10482-005-9039-5 Abstract >>
We have identified new members of the resuscitation-promoting factor (Rpf) protein family in numerous as yet unsequenced actinobacteria suggesting that Rpfs are common in this bacterial group. Formation and final delivery of the Rpf proteins varied from strain to strain and were dependent on growth conditions. Rpfs were found to act complementary to resuscitate other actinobacteria and might therefore be useful tools for the isolation of new actinobacterial species, especially from soil samples in which lots of microorganisms may have adopted dormant states.
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6. |
Amarita F,
Yvon M,
Nardi M,
Chambellon E,
Delettre J,
Bonnarme P,
( 2004 ) Identification and functional analysis of the gene encoding methionine-gamma-lyase in Brevibacterium linens. PMID : 15574935 : DOI : 10.1128/AEM.70.12.7348-7354.2004 PMC : PMC535188 Abstract >>
The enzymatic degradation of L-methionine and subsequent formation of volatile sulfur compounds (VSCs) is believed to be essential for flavor development in cheese. L-methionine-gamma-lyase (MGL) can convert L-methionine to methanethiol (MTL), alpha-ketobutyrate, and ammonia. The mgl gene encoding MGL was cloned from the type strain Brevibacterium linens ATCC 9175 known to produce copious amounts of MTL and related VSCs. The disruption of the mgl gene, achieved in strain ATCC 9175, resulted in a 62% decrease in thiol-producing activity and a 97% decrease in total VSC production in the knockout strain. Our work shows that L-methionine degradation via gamma-elimination is a key step in the formation of VSCs in B. linens.
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7. |
( 1996 ) A Brevibacterium linens pRBL1 replicon functional in Corynebacterium glutamicum. PMID : 8938050 : DOI : 10.1006/plas.1996.0029 Abstract >>
Brevibacterium linens RBL strain cryptic plasmid pRBL1 (8.0 kb) is described. A region involved in pRBL1 autonomous replication in Corynebacterium glutamicum was identified by insertion and deletion mapping and partially sequenced. This region encodes for a hypothetical 310-amino acid (aa) protein closely related to the replicases of plasmids pXZ10142 (C. glutamicum) and pAL5000 (Mycobacterium fortuitum). The 310-aa protein also shows significant homology to proteins of pColE5-099 (Shigella sonnei) and pJD1 (Neisseria gonorrhoea). At least one of these proteins, the Rep protein of pColE5-099, is known to be involved in theta replication.
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8. |
( 1996 ) Nucleotide sequence and taxonomical distribution of the bacteriocin gene lin cloned from Brevibacterium linens M18. PMID : 8919789 : PMC : PMC167894 Abstract >>
Linocin M18 is an antilisterial bacteriocin produced by the red smear cheese bacterium Brevibacterium linens M18. Oligonucleotide probes based on the N-terminal amino acid sequence were used to locate its single copy gene, lin, on the chromosomal DNA. The amino acid composition, N-terminal sequence, and molecular mass derived from the nucleotide sequence of an open reading frame of 798 nucleotides coding for 266 amino acids found on a 3-kb BamHI restriction fragment correspond closely to those obtained from the purified protein (N. Vald?s-Stauber and S. Scherer, Appl. Environ. Microbiol. 60:3809-3814, 1994). No sequence homology to any protein or nucleotide sequences deposited in databases was found. Comparison of the nucleotide sequence and the N-terminal amino acid sequence derived from the protein suggests that B. linens M18 produces an N-formyl-methionyl-CAC tRNA. A wide taxonomical distribution of the gene within coryneform bacteria has been demonstrated by PCR amplification. The structural gene from linocin M18 is present at least in three Brevibacterium species, five Arthrobacter species, and five Corynebacterium species.
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9. |
( N/A ) Phylogenetic relationships of Bacteria based on comparative sequence analysis of elongation factor Tu and ATP-synthase beta-subunit genes. PMID : 8085791 : DOI : 10.1007/bf00873088 Abstract >>
Comparative sequence analyses were performed on 14 genes encoding bacterial elongation factors EF-Tu and 7 genes encoding the beta-subunit of bacterial F1F0 type ATP-synthases. The corresponding predicted amino acid sequences were compared with published primary structures of homologous molecules. Phylogenetic trees were reconstructed from both data sets of aligned protein sequences and from an equivalent selection of 16S rRNA sequences by applying distance matrix and maximum parsimony methods. The EF-Tu data were in very good agreement with the rRNA data, although the resolution within the EF-Tu tree was reduced at certain phylogenetic levels. The resolution power of the ATPase beta-subunit sequence data were more reduced than those of the EF-Tu data. In comparison with the 16S rRNA tree there are minor differences in the order of adjacent branchings within the ATPase beta-subunit tree.
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10. |
( 1994 ) Isolation and characterization of Linocin M18, a bacteriocin produced by Brevibacterium linens. PMID : 7986050 : PMC : PMC201890 Abstract >>
Brevibacterium linens M18, isolated from red smear cheese, produces a substance that inhibits the growth of Listeria spp. and several coryneform and other gram-positive bacteria. No gram-negative bacteria were inhibited. The substance is heat labile, sensitive to proteolytic enzymes, and stable between pH 3 and 12. High levels of this bacteriocin, named Linocin M18, were obtained in the stationary growth phase. Linocin M18 was purified by ultrafiltration, ultracentrifugation, and gel filtration chromatography. In its native form, it is a proteinaceous aggregate with a high molecular weight. Fractions with Linocin M18 activity contained particles of 20 to 30 nm in diameter. The bacteriocin consists of a single protein subunit with a molecular mass of 31 kDa and an isoelectric point of 4.5 N-terminal sequence analysis yielded Met-Asn-Asn-Leu-Tyr-Arg-Glu-Leu-Ala-Pro-Ile-Pro-Gly-Pro-Ala-Ala-Ala-Glu- Ile. Significant homology with published sequences was lacking.
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