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1. Hoshino  Y, Nakamori  S, Takagi  H,     ( 2003 )

Cloning and analysis of the beta-lactamase gene from epsilon-poly-L-lysine-producing actinomycete Streptomyces albulus IFO14147.

Journal of biochemistry 134 (3)
PMID : 14561734  :   DOI  :   10.1093/jb/mvg166    
Abstract >>
Streptomyces albulus IFO14147 produces epsilon-poly-L-lysine, which exhibits antimicrobial activity. It is necessary for its molecular breeding to develop host-vector systems. We recently found a novel cryptic plasmid, pNO33, in this strain. As part of a search for a selectable marker gene for pNO33, we report here the isolation and analysis of the beta-lactamase gene of this strain, which can grow on ampicillin-containing plates. It was shown that the beta-lactamase production in S. albulus was induced by ampicillin. By introducing a genomic library of S. albulus into Escherichia coli, a 3.6-kbp fragment was identified as the region involved in ampicillin resistance. It contained three open reading frames, all of which are highly homologous to the beta-lactamase (the blaL product) and its regulatory proteins (the blaA and blaB products) of S. cacaoi. The growth phenotypes and enzyme assaying of E. coli and S. lividans showed that the blaL homologue (blaSa) encodes a beta-lactamase required for ampicillin resistance. The beta-lactamae gene can be utilized as a selectable marker in a cloning vector of S. albulus. However, the beta-lactamase activity was decreased in E. coli and repressed in S. lividans by the blaA and blaB homologues (blaASa and blaBSa). It appears as if the blaASa product is a repressor of blaSa instead of an activator as in S. cacaoi.
KeywordMeSH Terms
Cloning, Molecular
2. Hamano  Y, Yoshida  T, Kito  M, Nakamori  S, Nagasawa  T, Takagi  H,     ( 2006 )

Biological function of the pld gene product that degrades epsilon-poly-L-lysine in Streptomyces albulus.

Applied microbiology and biotechnology 72 (1)
PMID : 16568315  :   DOI  :   10.1007/s00253-006-0396-4    
Abstract >>
Epsilon-poly-L-lysine (epsilon-PL) is one of the few naturally occurring biopolymers and is characterized by a peptide bond between the alpha-carboxyl and epsilon-amino groups. Previously, we purified and characterized the epsilon-PL-degrading enzyme (Pld) from Streptomyces albulus, which is an epsilon-PL producer, and this enzyme was expected to confer self-resistance to the epsilon-PL produced by the organism itself. The gene encoding Pld was cloned based on the N-terminal amino acid sequence determined in this study, and a sequencing analysis revealed eight open reading frames (ORFs), i.e., ORF1 to ORF8 in the flanking region surrounding the pld gene (present in ORF5). To investigate the biological function of Pld, we constructed a knockout mutant in which the pld gene is inactivated. Studies on epsilon-PL susceptibility, epsilon-PL-degrading activity, and epsilon-PL productivity demonstrated that the pld gene does play a partial role in self-resistance and that S. albulus was found to produce other epsilon-PL-degrading enzyme(s) in addition to Pld. To the best of our knowledge, this is the first report on a self-resistance gene for a biopolymer possessing antibacterial activity.
KeywordMeSH Terms
3. Hamano  Y, Matsuura  N, Kitamura  M, Takagi  H,     ( 2006 )

A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific.

The Journal of biological chemistry 281 (25)
PMID : 16641084  :   DOI  :   10.1074/jbc.M602294200    
Abstract >>
Streptothricins (STs) produced by Streptomyces strains are broad-spectrum antibiotics. All STs consist of a carbamoylated D-gulosamine to which the beta-lysine homopolymer (1 to 7 residues) and the amide form of the unusual amino acid streptolidine (streptolidine lactam) are attached. Although many ST-resistance genes have been identified in bacteria, including clinically isolated pathogens and ST-producing Streptomyces strains, only one resistance mechanism has been identified to date. This mechanism involves the modification of the ST molecule by monoacetylation of the moiety of the beta-lysine(s). In this study, we successfully isolated a novel ST-resistance gene (sttH) from Streptomyces albulus, which is a known ST nonproducer. The in vitro analysis of SttH demonstrated that this enzyme catalyzes the hydrolysis of the amide bond of streptolidine lactam, thereby conferring ST resistance. Interestingly, the selective toxicity of ST-D possessing 3x beta-lysine moiety was altered from broad-spectrum to bacteria-specific by the hydrolysis of streptolidine lactam, although ST-F (1 x beta-lysine) was detoxified by SttH in both prokaryotes and eukaryotes (yeasts). STs have not been clinically developed due to their toxicities; however, in this study, we showed that hydrolyzed ST-D (ST-D-acid) exhibits potent antibacterial activity even when its toxicity against eukaryotic cells is reduced by SttH. This suggests that ST-D-acid is a potential candidate for clinical development or for use as a new lead compound for drug discovery.
KeywordMeSH Terms
Drug Resistance, Bacterial
4. Hamano  Y, Hoshino  Y, Nakamori  S, Takagi  H,     ( 2004 )

Overexpression and characterization of an aminoglycoside 6'-N-acetyltransferase with broad specificity from an epsilon-poly-L-lysine producer, Streptomyces albulus IFO14147.

Journal of biochemistry 136 (4)
PMID : 15625322  :   DOI  :   10.1093/jb/mvh146    
Abstract >>
Streptomyces albulus IFO14147 produces epsilon-poly-L-lysine, which exhibits antimicrobial activity. In the MIC studies with antibiotics, S. albulus IFO14147 was shown to be resistant to kanamycin and amikacin, which are aminoglycoside (AG) antibiotics. We report here the isolation of the AG-resistance gene from S. albulus IFO14147 and the substrate specificity of the gene product, AAC(6')-Isa, which catalyzes N-acetylation at the 6' position of AGs, thereby inactivating them. Kinetic studies revealed that this enzyme has remarkably wide substrate specificity. The V(max)/K(m) values determined for AGs vary by a factor of up to 6,300, a much wider range than those observed for the AAC(6')s from Enterococcus faecium [AAC(6')-Ii] and Salmonella enteritidis [AAC(6')-Iy]. In addition, AAC(6')-Isa was able to acetylate lividomycin A, which has a hydroxy group at the 6' position. Enzymatically acetylated lividomycin A was found to be highly susceptible to mild base hydrolysis, suggesting that the enzyme also catalyzes O-acetyltransfer.
KeywordMeSH Terms
5. Kim  BJ, Kim  CJ, Chun  J, Koh  YH, Lee  SH, Hyun  JW, Cha  CY, Kook  YH,     ( 2004 )

Phylogenetic analysis of the genera Streptomyces and Kitasatospora based on partial RNA polymerase beta-subunit gene (rpoB) sequences.

International journal of systematic and evolutionary microbiology 54 (Pt 2)
PMID : 15023980  :   DOI  :   10.1099/ijs.0.02941-0    
Abstract >>
The RNA polymerase beta-subunit genes (rpoB) of 67 Streptomyces strains, representing 57 species, five Kitasatospora strains and Micromonospora echinospora KCTC 9549 were partially sequenced using a pair of rpoB PCR primers. Among the streptomycetes, 99.7-100 % similarity within the same species and 90.2-99.3 % similarity at the interspecific level were observed by analysis of the determined rpoB sequences. The topology of the phylogenetic tree based on rpoB sequences was similar to that of 16S rDNA. The five Kitasatospora strains formed a stable monophyletic clade and a sister group to the clade comprising all Streptomyces species. Although there were several discrepancies in the details, considerable agreement was found between the results of rpoB analysis and those of numerical phenetic classification. This study demonstrates that analysis of rpoB can be used as an alternative genetic method in parallel to conventional taxonomic methods, including numerical phenetic and 16S rDNA analyses, for the phylogenetic analyses of the genera Streptomyces and Kitasatospora.
KeywordMeSH Terms
6. Maruyama  C, Hamano  Y,     ( 2009 )

The biological function of the bacterial isochorismatase-like hydrolase SttH.

Bioscience, biotechnology, and biochemistry 73 (11)
PMID : 19897889  :   DOI  :   10.1271/bbb.90499    
Abstract >>
The streptothricin hydrolase (SttH), which is a member of the isochorismatase-like hydrolase (ILH) super-family, catalyzes the hydrolysis of the streptolidine lactam group in streptothricin (ST) antibiotics, thereby inactivating them. In this study we identified a novel homologous gene (sttH-sn) and sequenced the flanking regions of the sttH and sttH-sn genes. The organization of genes around the sttH, sttH-sn, and ILH genes revealed that a number of the genes were clustered with genes encoding oxidoreductases with molybdopterin binding subunits, suggesting that the true role of these gene products (SttHs and a number of ILHs) might have to do with the chemical modification of molybdopterin, rather than ST-resistance. In addition, mutant enzymes were constructed in which Ser was substituted for highly conserved Cys-176 and Cys-158 of SttH and SttH-sn respectively, and no enzyme activities were detected. Thus, biochemically, these ILHs were found to be "cysteine hydrolases."
KeywordMeSH Terms
7. Yamanaka  K, Maruyama  C, Takagi  H, Hamano  Y,     ( 2008 )

Epsilon-poly-L-lysine dispersity is controlled by a highly unusual nonribosomal peptide synthetase.

Nature chemical biology 4 (12)
PMID : 18997795  :   DOI  :   10.1038/nchembio.125    
Abstract >>
Epsilon-Poly-L-lysine (epsilon-PL) consists of 25-35 L-lysine residues in isopeptide linkages and is one of only two amino acid homopolymers known in nature. Elucidating the biosynthetic mechanism of epsilon-PL should open new avenues for creating novel classes of biopolymers. Here we report the purification of an epsilon-PL synthetase (Pls; 130 kDa) and the cloning of its gene from an epsilon-PL-producing strain of Streptomyces albulus. Pls was found to be a membrane protein with adenylation and thiolation domains characteristic of the nonribosomal peptide synthetases (NRPSs). It had no traditional condensation or thioesterase domain; instead, it had six transmembrane domains surrounding three tandem soluble domains. These tandem domains iteratively catalyzed L-lysine polymerization using free L-lysine polymer (or monomer in the initial reaction) as acceptor and Pls-bound L-lysine as donor, directly yielding chains of diverse length. Thus, Pls is a new single-module NRPS having an amino acid ligase-like catalytic activity for peptide bond formation.
KeywordMeSH Terms
Peptide Biosynthesis, Nucleic Acid-Independent
8. Hamano  Y, Nicchu  I, Shimizu  T, Onji  Y, Hiraki  J, Takagi  H,     ( 2007 )

epsilon-Poly-L: -lysine producer, Streptomyces albulus, has feedback-inhibition resistant aspartokinase.

Applied microbiology and biotechnology 76 (4)
PMID : 17611754  :   DOI  :   10.1007/s00253-007-1052-3    
Abstract >>
Streptomyces albulus NBRC14147 produces epsilon-poly-L: -lysine (epsilon-PL), which is an amino acid homopolymer antibiotic. Despite the commercial importance of epsilon-PL, limited information is available regarding its biosynthesis; the L: -lysine molecule is directly utilized for epsilon-PL biosynthesis. In most bacteria, L: -lysine is biosynthesized by an aspartate pathway. Aspartokinase (Ask), which is the first enzyme in this pathway, is subject to complex regulation such as through feedback inhibition by the end-product amino acids such as L: -lysine and/or L: -threonine. S. albulus NBRC14147 can produce a large amount of epsilon-PL (1-3 g/l). We therefore suspected that Ask(s) of S. albulus could be resistant to feedback inhibition to provide sufficient L: -lysine for epsilon-PL biosynthesis. To address this hypothesis, in this study, we cloned the ask gene from S. albulus and investigated the feedback inhibition of its gene product. As predicted, we revealed the feedback resistance of the Ask; more than 20% relative activity of Ask was detected in the assay mixture even with extremely high concentrations of L: -lysine and L: -threonine (100 mM each). We further constructed a mutated ask gene for which the gene product Ask (M68V) is almost fully resistant to feedback inhibition. The homologous expression of Ask (M68V) further demonstrated the increase in epsilon-PL productivity.
KeywordMeSH Terms
9. Gu  Y, Yang  C, Wang  X, Geng  W, Sun  Y, Feng  J, Wang  Y, Quan  Y, Che  Y, Zhang  C, Gong  T, Zhang  W, Gao  W, Zuo  Z, Song  C, Wang  S,     ( 2014 )

Genome Sequence of the �`-Poly-l-Lysine-Producing Strain Streptomyces albulus NK660, Isolated from Soil in Gutian, Fujian Province, China.

Genome announcements 2 (3)
PMID : 24926050  :   DOI  :   10.1128/genomeA.00532-14     PMC  :   PMC4056293    
Abstract >>
We determined the complete genome sequence of a soil bacterium, Streptomyces albulus NK660. It can produce �`-poly-l-lysine, which has antimicrobial activity against a spectrum of microorganisms. The genome of S. albulus NK660 contains a 9,360,281-bp linear chromosome and a 12,120-bp linear plasmid.
KeywordMeSH Terms

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