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1.
Int J Mol Sci ; 22(8)2021 Apr 16.
Article in English | MEDLINE | ID: mdl-33923711

ABSTRACT

There has been a recent increase in the exploration of cold-active ß-galactosidases, as it offers new alternatives for the dairy industry, mainly in response to the current needs of lactose-intolerant consumers. Since extremophilic microbial compounds might have unique physical and chemical properties, this research aimed to study the capacity of Antarctic bacterial strains to produce cold-active ß-galactosidases. A screening revealed 81 out of 304 strains with ß-galactosidase activity. The strain Se8.10.12 showed the highest enzymatic activity. Morphological, biochemical, and molecular characterization based on whole-genome sequencing confirmed it as the first Rahnella inusitata isolate from the Antarctic, which retained 41-62% of its ß-galactosidase activity in the cold (4 °C-15 °C). Three ß-galactosidases genes were found in the R. inusitata genome, which belong to the glycoside hydrolase families GH2 (LacZ and EbgA) and GH42 (BglY). Based on molecular docking, some of these enzymes exhibited higher lactose predicted affinity than the commercial control enzyme from Aspergillus oryzae. Hence, this work reports a new Rahnella inusitata strain from the Antarctic continent as a prominent cold-active ß-galactosidase producer.


Subject(s)
Cold Temperature , Rahnella/enzymology , beta-Galactosidase/metabolism , Acclimatization , Enzyme Stability , Rahnella/genetics , beta-Galactosidase/chemistry , beta-Galactosidase/genetics
2.
Carbohydr Polym ; 162: 10-15, 2017 Apr 15.
Article in English | MEDLINE | ID: mdl-28224885

ABSTRACT

R-ß-Gal is a cold-adapted ß-galactosidase that is able to hydrolyze lactose and has the potential to produce low-lactose or lactose-free dairy products at low temperatures (4°C). Cold-adapted enzymes unfold at moderate temperatures due to the lower intramolecular stabilizing interactions necessary for flexibility at low temperatures. To increase stability and usage-performance, R-ß-Gal was encapsulated in gellan gum by injecting an aqueous solution into two different hardening solutions (10mM CaCl2 or 10mM MgCl2). Enzyme characteristics of both free and encapsulated R-ß-Gal were carried out, and the different effects of two cations were investigated. R-ß-Gal showed better thermal and pH stability after encapsulation. Ca2+ gels had higher encapsulation efficiency (71.4%) than Mg2+ (66.7%) gels, and Ca2+ formed larger inner and surface pores. R-ß-Gal was released from the Ca2+ hydrogel beads more rapidly than the Mg2+ hydrogels during storage in aqueous solution due to the larger inner/surface pores of the matrix.


Subject(s)
Microspheres , Polysaccharides, Bacterial/chemistry , Rahnella/enzymology , beta-Galactosidase/metabolism , Cold Temperature
3.
Protein Expr Purif ; 115: 158-64, 2015 Nov.
Article in English | MEDLINE | ID: mdl-26145832

ABSTRACT

A novel gene was isolated for the first time from a psychrophilic gram-negative bacterium Rahnella sp. R3. The gene encoded a cold-adapted ß-galactosidase (R-ß-Gal). Recombinant R-ß-Gal was expressed in Escherichia coli BL21 (DE3), purified and characterized. R-ß-gal belongs to the glycosyl hydrolase family 42. Circular dichroism spectrometry of the structural stability of R-ß-Gal with respect to temperature indicated that the secondary structures of the enzyme were stable to 45°C. In solution, the enzyme was a homo-trimer and was active at temperatures as low as 4°C. The enzyme did not require the presence of metal ions to be active, but Mg(2+), Mn(2+), and Ca(2+) enhanced its activity slightly, whereas Fe(3+), Zn(2+) and Al(3+) appeared to inactive it. The purified enzyme displayed K(m) values of 6.5 mM for ONPG and 2.2mM for lactose at 4°C. These values were lower than the corresponding K(m)s reported for other cold-adapted ß-Gals.


Subject(s)
Rahnella/enzymology , Recombinant Proteins/chemistry , Recombinant Proteins/metabolism , beta-Galactosidase/chemistry , beta-Galactosidase/metabolism , Cloning, Molecular , Cold Temperature , Enzyme Stability , Escherichia coli/genetics , Hydrogen-Ion Concentration , Kinetics , Metals, Heavy , Rahnella/genetics , Recombinant Proteins/genetics , Recombinant Proteins/isolation & purification , beta-Galactosidase/genetics , beta-Galactosidase/isolation & purification
4.
Bioprocess Biosyst Eng ; 36(6): 757-63, 2013 Jun.
Article in English | MEDLINE | ID: mdl-23361186

ABSTRACT

In the present study, we developed an efficient method of 1,3-propanediol (1,3-PD) production from glycerol by genetic engineering of Klebsiella pneumoniae AK mutant strains. The proposed approach eliminated by-product formation and IPTG induction resulted in maximal production of 1,3-PD. A series of recombinant strains was designed to constitutively express the dhaB and/or dhaT genes, using the bacteriophage T5 P(DE20) promoter and the rho-independent transcription termination signal of the Rahnella aquatilis levansucrase gene. Among these strains, AK/pConT expressing dhaT alone gave the highest yield of 1,3-PD. Fed-batch fermentation resulted in efficient production of 1,3-PD from either pure or crude glycerol, without by-product formation.


Subject(s)
Alcohol Dehydrogenase/biosynthesis , Bacterial Proteins/biosynthesis , Gene Expression , Glycerol/metabolism , Klebsiella pneumoniae/metabolism , Metabolic Engineering , Propylene Glycols/metabolism , Alcohol Dehydrogenase/genetics , Bacterial Proteins/genetics , Bacteriophages/genetics , Bacteriophages/metabolism , Cryoprotective Agents/metabolism , Cryoprotective Agents/pharmacology , Glycerol/pharmacology , Hexosyltransferases/biosynthesis , Hexosyltransferases/genetics , Klebsiella pneumoniae/genetics , Promoter Regions, Genetic , Rahnella/enzymology , Rahnella/genetics , Viral Proteins/biosynthesis , Viral Proteins/genetics
5.
Folia Microbiol (Praha) ; 58(3): 201-10, 2013 May.
Article in English | MEDLINE | ID: mdl-23054688

ABSTRACT

Plagiodera versicolora (Laicharting, 1781) (Coleoptera: Chrysomelidae) is an important forest pest which damages many trees such as willow, poplar, and hazelnut. In order to find new microbes that can be utilized as a possible microbial control agent against this pest, we investigated the culturable bacterial flora of it and tested the isolated bacteria against P. versicolora larvae and adults. We were able to isolate nine bacteria from larvae and adults. The isolates were characterized using a combination of morphological, biochemical, and physiological methods. Additionally, we sequenced the partial sequence of the 16S rRNA gene to verify conventional identification results. Based on characterization studies, the isolates were identified as Staphylococcus sp. Pv1, Rahnella sp. Pv2, Rahnella sp. Pv3, Rahnella sp. Pv4, Rahnella sp. Pv5, Pantoea agglomerans Pv6, Staphylococcus sp. Pv7, Micrococcus luteus Pv8, and Rahnella sp. Pv9. The highest insecticidal activity against larvae and adults was obtained from M. luteus Pv8 with 50 and 40 % mortalities within 10 days after treatment, respectively. Extracellular enzyme activity of the bacterial isolates such as amylase, proteinase, lipase, cellulose, and chitinase was also determined. Consequently, our results show that M. luteus Pv8 might be a good candidate as a possible microbial control agent against P. versicolora and were discussed with respect to biocontrol potential of the bacterial isolates.


Subject(s)
Coleoptera/microbiology , Microbiota , Micrococcus luteus/isolation & purification , Pantoea/isolation & purification , Rahnella/isolation & purification , Staphylococcus/isolation & purification , Amylases/metabolism , Animals , Biological Control Agents , Cellulose/metabolism , Chitinases/metabolism , Larva/microbiology , Lipase/metabolism , Microbial Sensitivity Tests , Micrococcus luteus/enzymology , Micrococcus luteus/pathogenicity , Pantoea/enzymology , Pantoea/pathogenicity , Peptide Hydrolases/metabolism , Phenotype , RNA, Ribosomal, 16S/genetics , Rahnella/enzymology , Rahnella/pathogenicity , Sequence Analysis, DNA , Staphylococcus/enzymology , Staphylococcus/pathogenicity , Virulence
6.
PLoS One ; 7(8): e39579, 2012.
Article in English | MEDLINE | ID: mdl-22870190

ABSTRACT

The 5-enolpyruvylshikimate-3-phosphate synthase (EPSPS; EC 2.5.1.19) is a key enzyme in the shikimate pathway for the production of aromatic amino acids and chorismate-derived secondary metabolites in plants, fungi, and microorganisms. It is also the target of the broad-spectrum herbicide glyphosate. Natural glyphosate resistance is generally thought to occur within microorganisms in a strong selective pressure condition. Rahnella aquatilis strain GR20, an antagonist against pathogenic agrobacterial strains of grape crown gall, was isolated from the rhizosphere of grape in glyphosate-contaminated vineyards. A novel gene encoding EPSPS was identified from the isolated bacterium by complementation of an Escherichia coli auxotrophic aroA mutant. The EPSPS, named AroA(R. aquatilis), was expressed and purified from E. coli, and key kinetic values were determined. The full-length enzyme exhibited higher tolerance to glyphosate than the E. coli EPSPS (AroA(E. coli)), while retaining high affinity for the substrate phosphoenolpyruvate. Transgenic plants of AroA(R. aquatilis) were also observed to be more resistant to glyphosate at a concentration of 5 mM than that of AroA(E. coli). To probe the sites contributing to increased tolerance to glyphosate, mutant R. aquatilis EPSPS enzymes were produced with the c-strand of subdomain 3 and the f-strand of subdomain 5 (Thr38Lys, Arg40Val, Arg222Gln, Ser224Val, Ile225Val, and Gln226Lys) substituted by the corresponding region of the E. coli EPSPS. The mutant enzyme exhibited greater sensitivity to glyphosate than the wild type R. aquatilis EPSPS with little change of affinity for its first substrate, shikimate-3-phosphate (S3P) and phosphoenolpyruvate (PEP). The effect of the residues on subdomain 5 on glyphosate resistance was more obvious.


Subject(s)
3-Phosphoshikimate 1-Carboxyvinyltransferase , Bacterial Proteins , Drug Resistance, Bacterial/physiology , Enzyme Inhibitors/pharmacology , Glycine/analogs & derivatives , Rahnella , 3-Phosphoshikimate 1-Carboxyvinyltransferase/genetics , 3-Phosphoshikimate 1-Carboxyvinyltransferase/metabolism , Amino Acid Sequence , Amino Acid Substitution , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Base Sequence , Glycine/pharmacology , Molecular Sequence Data , Mutation, Missense , Plant Diseases/microbiology , Protein Structure, Tertiary , Rahnella/enzymology , Rahnella/genetics , Substrate Specificity , Vitis/microbiology , Glyphosate
7.
Plasmid ; 65(1): 70-6, 2011 Jan.
Article in English | MEDLINE | ID: mdl-20854841

ABSTRACT

pHW126, pIGRK, pIGMS31 and pRAO1 are the only known members of a novel and as yet uncharacterised family of rolling circle plasmids. pHW126 contains only two open reading frames, of which one shows homology to pMV158-family mobilisation proteins. Here we provide evidence that the second open reading frame encodes a replication protein (Rep). Mutation or deletion of this gene resulted in replication deficient constructs, but providing functional Rep from a compatible vector rescued these constructs, indicating that Rep acts in trans. An approximately 300 bp cis-acting region representing the origin of replication was identified upstream of the rep gene. The origin was identified to be composed of three parts: an accessory region, a conserved stretch and four perfect tandem repeats. The two latter elements were essential for replication. Constructs with a deletion of the accessory region could still replicate, but their loss rate was high, indicating that the accessory region is necessary for plasmid maintenance under non-selective conditions. Interestingly, pHW126 could replicate in all Enterobacteriaceae tested while Agrobacterium tumefaciens and Pseudomonas syringae were inappropriate hosts. Thus, pHW126 seems to have a rather limited host range.


Subject(s)
DNA, Circular/genetics , Plasmids/genetics , Regulatory Sequences, Nucleic Acid/genetics , Base Sequence , DNA Replication/genetics , Deoxyribonuclease I/metabolism , Genes, Bacterial/genetics , Host Specificity/genetics , Molecular Sequence Data , Open Reading Frames/genetics , Rahnella/enzymology , Rahnella/genetics , Replication Origin/genetics
8.
J Antimicrob Chemother ; 65(8): 1619-23, 2010 Aug.
Article in English | MEDLINE | ID: mdl-20511369

ABSTRACT

OBJECTIVES: Rahnella aquatilis is an environmental enterobacterial species with a chromosomal bla(RAHN-1) gene encoding extended-spectrum class A beta-lactamase RAHN-1. We describe the diversity of bla(RAHN) genes from two groups of strains, G1 and G2, isolated from raw fruits and vegetables, and the new class A beta-lactamase RAHN-2. METHODS: MICs were determined by Etest. bla(RAHN) genes were amplified by PCR, sequenced, and cloned to produce RAHN-1 and RAHN-2 proteins whose kinetic parameters were determined. RESULTS: All strains had similar beta-lactam resistance patterns. However, isolates of G1 were at least 2-fold more susceptible to piperacillin, amoxicillin, piperacillin/clavulanic acid, piperacillin/tazobactam and cefotaxime. Sequences of bla(RAHN) from G1 had <82.9% identity with that of bla(RAHN-1), whereas those of G2 were >92% identical. The RAHN-2 beta-lactamase was 89.8% identical to RAHN-1, 5-fold more efficient than RAHN-1 in hydrolysing ticarcillin and 2.5-fold more efficient in cefotaxime and cefuroxime hydrolysis. However, the specific activity of RAHN-1 was 2-fold higher than that of RAHN-2 suggesting that the bla(RAHN) genes are regulated differently. CONCLUSIONS: The new class A beta-lactamase RAHN-2 is phenotypically difficult to detect and requires MIC determination.


Subject(s)
Bacterial Proteins/biosynthesis , Bacterial Proteins/genetics , Polymorphism, Genetic , Rahnella/enzymology , beta-Lactamases/biosynthesis , beta-Lactamases/genetics , Anti-Bacterial Agents/pharmacology , DNA, Bacterial/chemistry , DNA, Bacterial/genetics , Fruit/microbiology , Kinetics , Microbial Sensitivity Tests , Phylogeny , Polymerase Chain Reaction , Rahnella/drug effects , Sequence Analysis, DNA , Sequence Homology, Amino Acid , Vegetables/microbiology , beta-Lactamases/metabolism , beta-Lactams/metabolism , beta-Lactams/pharmacology
9.
Environ Microbiol ; 9(12): 3122-33, 2007 Dec.
Article in English | MEDLINE | ID: mdl-17991039

ABSTRACT

In this study, the immobilization of toxic uranium [U(VI)] mediated by the intrinsic phosphatase activities of naturally occurring bacteria isolated from contaminated subsurface soils was examined. The phosphatase phenotypes of strains belonging to the genera, Arthrobacter, Bacillus and Rahnella, previously isolated from subsurface soils at the US Department of Energy's (DOE) Oak Ridge Field Research Center (ORFRC), were determined. The ORFRC represents a unique, extreme environment consisting of highly acidic soils with co-occurring heavy metals, radionuclides and high nitrate concentrations. Isolates exhibiting phosphatase-positive phenotypes indicative of constitutive phosphatase activity were subsequently tested in U(VI) bioprecipitation assays. When aerobically grown in synthetic groundwater (pH 5.5) amended with 10 mM glycerol-3-phosphate (G3P), phosphatase-positive Bacillus and Rahnella spp. strains Y9-2 and Y9602 liberated sufficient phosphate to precipitate 73% and 95% of total soluble U added as 200 microM uranyl acetate respectively. In contrast, an Arthrobacter sp. X34 exhibiting a phosphatase-negative phenotype did not liberate phosphate from G3P or promote U(VI) precipitation. This study provides the first evidence of U(VI) precipitation via the phosphatase activity of naturally occurring Bacillus and Rahnella spp. isolated from the acidic subsurface at the DOE ORFRC.


Subject(s)
Bacillus , Phosphates/chemistry , Rahnella , Soil Microbiology , Soil Pollutants, Radioactive/chemistry , Uranium/chemistry , Aerobiosis , Bacillus/drug effects , Bacillus/enzymology , Bacillus/genetics , Bacillus/isolation & purification , Biodegradation, Environmental , Chemical Precipitation , Drug Resistance, Bacterial , Metals/pharmacology , Molecular Sequence Data , Phosphates/metabolism , Phosphoric Monoester Hydrolases/metabolism , Rahnella/drug effects , Rahnella/enzymology , Rahnella/genetics , Rahnella/isolation & purification , Sequence Analysis, DNA , Soil Pollutants/metabolism , Soil Pollutants, Radioactive/metabolism , Water Pollutants, Radioactive/metabolism
10.
J Microbiol ; 44(4): 396-402, 2006 Aug.
Article in English | MEDLINE | ID: mdl-16953174

ABSTRACT

beta-Galactosidase is extensively employed in the manufacture of dairy products, including lactose-reduced milk. Here, we have isolated two gram-negative and rod-shaped coldadapted bacteria, BS 1 and HS 39. These strains were able to break down lactose at low temperatures. Although two isolates were found to grow well at 10 degrees , the BS 1 strain was unable to grow at 37 degrees . Another strain, HS-39, evidenced retarded growth at 37 degrees . The biochemical characteristics and the results of 16S rDNA sequencing identified the BS 1 isolate as Rahnella aquatilis, and showed that the HS 39 strain belonged to genus Buttiauxella. Whereas the R. aquatilis BS 1 strain generated maximal quantities of beta-galactosidase when incubated for 60 h at 10 degrees , Buttiauxella sp. HS-39 generated beta-galactosidase earlier, and at slightly lower levels, than R. aquatilis BS 1. The optimum temperature for beta-galactosidase was 30 degrees for R. aquatilis BS-1, and was 45 degrees for Buttiauxella sp. HS-39, thereby indicating that R. aquatilis BS-1 was able to generate a cold-adaptive enzyme. These two cold-adapted strains, and most notably the beta-galactosidase from each isolate, might prove useful in some biotechnological applications.


Subject(s)
Enterobacteriaceae/isolation & purification , Lactose/metabolism , Rahnella/isolation & purification , beta-Galactosidase/metabolism , Cold Temperature , Enterobacteriaceae/classification , Enterobacteriaceae/enzymology , Enterobacteriaceae/growth & development , Phylogeny , RNA, Ribosomal, 16S/genetics , Rahnella/classification , Rahnella/enzymology , Rahnella/growth & development , beta-Galactosidase/biosynthesis , beta-Galactosidase/chemistry
11.
J Bacteriol ; 184(21): 5862-70, 2002 Nov.
Article in English | MEDLINE | ID: mdl-12374819

ABSTRACT

Expression of the lsrA gene from Rahnella aquatilis, encoding levansucrase, is tightly regulated by the growth phase of the host cell; low-level expression was observed in the early phase of cell growth, but expression was significantly stimulated in the late phase. Northern blot analysis revealed that regulation occurred at the level of transcription. The promoter region was identified by primer extension analysis. Two opposite genetic elements that participate in the regulation of lsrA expression were identified upstream of the lsrA gene: the lsrS gene and the lsrR region. The lsrS gene encodes a protein consisting of 70 amino acid residues (M(r), 8,075), which positively activated lsrA expression approximately 20-fold in a growth phase-dependent fashion. The cis-acting lsrR region, which repressed lsrA expression about 10-fold, was further narrowed to two DNA regions by deletion analysis. The concerted action of two opposite regulatory functions resulted in the growth phase-dependent activation of gene expression in Escherichia coli independent of the stationary sigma factor sigma(S).


Subject(s)
Gene Expression Regulation, Bacterial , Gene Expression Regulation, Enzymologic , Hexosyltransferases/genetics , Rahnella/enzymology , Amino Acid Sequence , Bacteriophage P2 , Base Sequence , Binding Sites , DNA, Bacterial , Escherichia coli/growth & development , Genes, Bacterial , Molecular Sequence Data , Rahnella/genetics , Rahnella/growth & development , Repressor Proteins/genetics , Repressor Proteins/metabolism , Trans-Activators/genetics , Trans-Activators/metabolism , Transcription Initiation Site
12.
Biosci Biotechnol Biochem ; 66(11): 2474-8, 2002 Nov.
Article in English | MEDLINE | ID: mdl-12506991

ABSTRACT

Five gram-negative bacteria, all of which were Enterobacteriaceae, were isolated from the phyllosphere of green or senescing leaves of Rosa rugosa, and their phenotypic and physiological characteristics were examined. Partial 16S rDNA sequences led to identification of these isolates as Pantoea agglomerans, Klebsiella terrigena, Erwinia rhapontici, and two strains of Rahnella aquatilis. Interestingly, these phyllosphere bacteria had certain phenotypic and physiological convergences, while they showed their own metabolic properties toward phenolic compounds of plant origin. In particular, the two Ra. aquatilis isolates from the green leaves had a substrate-inducible gallate decarboxylase activity in the resting cells that had been cultured in 1 mM gallic acid- or protocatechuic acid-containing medium. The other three isolates from the senescing leaves did not have this enzyme activity. Simple phenolics that the Ra. aquatilis decarboxylatively produced from benzoic acid derivatives had better antimicrobial activities than those of the substrates.


Subject(s)
Enterobacteriaceae/classification , Enterobacteriaceae/metabolism , Plant Leaves/microbiology , Rosaceae/microbiology , Antifungal Agents , Carboxy-Lyases/metabolism , Catechols/pharmacology , DNA, Ribosomal/genetics , Decarboxylation , Enterobacteriaceae/genetics , Enterobacteriaceae/isolation & purification , Gallic Acid/metabolism , Hydroxybenzoates/metabolism , Hydroxybenzoates/pharmacology , Phenols/chemistry , Phenols/metabolism , Phenotype , RNA, Bacterial/genetics , RNA, Ribosomal, 16S/genetics , Rahnella/enzymology
13.
Antimicrob Agents Chemother ; 45(10): 2965-8, 2001 Oct.
Article in English | MEDLINE | ID: mdl-11557504

ABSTRACT

From whole-cell DNA of a clinical isolate of the enterobacterial species Rahnella aquatilis, a beta-lactamase gene was cloned that encoded a chromosomally encoded Ambler class A enzyme, RAHN-1. RAHN-1, with a pI of 7.2, shares 76, 73, and 71% amino acid identity with the extended-spectrum beta-lactamase of chromosomal origin from Serratia fonticola and with the plasmid-mediated beta-lactamases CTX-M-2 and CTX-M-1, respectively. The hydrolysis spectrum of the clavulanic acid-inhibited RAHN-1 was expanded to cephalosporins such as cefuroxime, cefotaxime, and ceftriaxone, but not to ceftazidime. Its expression was not inducible.


Subject(s)
Chromosomes, Bacterial , Rahnella/genetics , beta-Lactamases/genetics , Amino Acid Sequence , Cephalosporins/metabolism , Cloning, Molecular , Humans , Microbial Sensitivity Tests , Molecular Sequence Data , Rahnella/drug effects , Rahnella/enzymology , Sequence Homology, Amino Acid , beta-Lactamases/metabolism , beta-Lactams/pharmacology
14.
J Biotechnol ; 81(1): 63-72, 2000 Jul 28.
Article in English | MEDLINE | ID: mdl-10936661

ABSTRACT

A levansucrase gene (lsrA) from Rahnella aquatilis ATCC33071 was isolated from a genomic library and the nucleotide sequence of the lsrA structural gene was determined. lsrA is composed of 1248 bp and encodes 415 amino acid residues with a calculated molecular mass of 45.9 kDa. Although the amino acid sequence of lsrA gene showed good conservation with the sequences of reported levansucrases and of the conserved regions thought to be implicated in the enzyme activity, comparison of the deduced amino acid sequences certified the dissimilarity of the proteins from Gram-negative and Gram-positive bacteria. The lsrA gene was expressed from its own promoter in Escherichia coli in an active form. The lsrA expression in E. coli-pRL1CPR was affected by the growth phase of cells: it was repressed in the early phase of growth, but was significantly stimulated during the entrance of cells into the late phase of growth. The growth-phase-dependent fashion of lsrA expression was altered in a constitutive-like fashion by the deletion of an upstream region of lsrA (pNd137), suggesting that the growth-phase dependent expression of lsrA was mediated by the deleted upstream region.


Subject(s)
Escherichia coli/genetics , Hexosyltransferases/genetics , Hexosyltransferases/metabolism , Rahnella/genetics , Amino Acid Sequence , Base Sequence , Cell Division/genetics , Cloning, Molecular , Molecular Sequence Data , Rahnella/enzymology , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Sequence Analysis , Sequence Homology, Amino Acid
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