Propionibacteria

Vorobjeva, Lena I.

doi:10.1007/978-94-017-2803-4

Cited by 41 publications

(40 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…freudenreichii grown under nonselective conditions. Successful manipulation of a host-vector system in propionibacteria should facilitate genetic studies and lead to creation of genes that are useful industrially.Propionibacteria, which have a wide range of probiotic activity, are used in making dairy foods, such as cheese, for the production of vitamin B 12 , tetrapyrrole compounds, and propionic acid (8,15,21), in bread baking, as starters for ensilage, and in some pharmaceutical preparations (35). To elucidate the biosynthetic pathways of vitamin B 12 and siroheme in Propionibacterium, we previously identified several genes coding for the enzymes involved in production of tetrapyrrole derivatives (hemYHBXRL) (11,12) and vitamin B 12 (cobA, cbiO) (30).…”

mentioning

confidence: 99%

“…On the basis of this information concerning pRGO1, we succeeded in constructing a useful shuttle vector for shuttling between Propionibacterium cells and E. coli using regions including orf1, orf2, orf5, and orf6 of pRGO1 and pUC18. Although several attempts have been made to develop a transformation system in propionibacteria, a successful transformation system suitable for practical use has not been reported previously (35). This may be due to the selection marker and the existence of a strong restriction-modification system in propionibacteria.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Characterization of pRGO1, a Plasmid from Propionibacterium acidipropionici , and Its Use for Development of a Host-Vector System in Propionibacteria

Kiatpapan

Hashimoto

Nakamura

et al. 2000

Appl Environ Microbiol

View full text Add to dashboard Cite

The complete nucleotide sequence of pRGO1, a cryptic plasmid from Propionibacterium acidipropionici E214, was determined. pRGO1 is 6,868 bp long, and its G؉C content is 65.0%. Frame analysis of the sequence revealed six open reading frames, which were designated Orf1 to Orf6. The deduced amino acid sequences of Orf1 and Orf2 showed extensive similarities to an initiator of plasmid replication, the Rep protein, of various plasmids of gram-positive bacteria. The amino acid sequence of the putative translation product of orf3 exhibited a high degree of similarity to the amino acid sequences of DNA invertase in several bacteria. For the putative translation products of orf4, orf5, and orf6, on the other hand, no homologous sequences were found. The function of these open reading frames was studied by deletion analysis. A shuttle vector, pPK705, was constructed for shuttling between Escherichia coli and a Propionibacterium strain containing orf1 (repA), orf2 (repB), orf5, and orf6 from pRGO1, pUC18, and the hygromycin B-resistant gene as a drug marker. Shuttle vector pPK705 successfully transformed Propionibacterium freudenreichii subsp. shermanii IFO12426 by electroporation at an efficiency of 8 ؋ 10 6 CFU/g of DNA under optimized conditions. Transformation of various species of propionibacteria with pPK705 was also performed at efficiencies of about 10 4 to 10 7 CFU/g of DNA. The vector was stably maintained in strains of P. freudenreichii subsp. shermanii, P. freudenreichii, P. pentosaceum, and P. freudenreichii subsp. freudenreichii grown under nonselective conditions. Successful manipulation of a host-vector system in propionibacteria should facilitate genetic studies and lead to creation of genes that are useful industrially.Propionibacteria, which have a wide range of probiotic activity, are used in making dairy foods, such as cheese, for the production of vitamin B 12 , tetrapyrrole compounds, and propionic acid (8,15,21), in bread baking, as starters for ensilage, and in some pharmaceutical preparations (35). To elucidate the biosynthetic pathways of vitamin B 12 and siroheme in Propionibacterium, we previously identified several genes coding for the enzymes involved in production of tetrapyrrole derivatives (hemYHBXRL) (11,12) and vitamin B 12 (cobA, cbiO) (30).Development of genetic manipulation in propionibacteria has progressed slowly due to a lack of detailed information on the genetics of the bacteria and a lack of an appropriate plasmid that can serve as a possible transformation vector. A number of plasmids from Propionibacterium acidipropionici, P. freudenreichii, and P. jensenii, ranging in size from 4.4 to more than 119 MDa, have been described (19,24). However, neither analysis of a plasmid DNA sequence nor construction of a vector for propionibacteria has been reported. To establish a versatile vector system to facilitate genetic analysis and to allow the transfer of a gene of interest, we investigated the development of a host-vector system in propionibacteria.We succeeded in determining the co...

show abstract

mentioning

confidence: 99%

mentioning

confidence: 99%

Characterization of pRGO1, a Plasmid from Propionibacterium acidipropionici , and Its Use for Development of a Host-Vector System in Propionibacteria

Kiatpapan

Hashimoto

Nakamura

et al. 2000

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

“…"# is produced commercially by two organisms, Pseudomonas denitrificans and Propionibacterium freudenreichii (P. shermanii) (Vorobjeva, 2000). The genes that determine the aerobic biosynthetic route to B "# in Ps.…”

Section: Vitamin Bmentioning

confidence: 99%

“…1b) would be an ideal location for the observed inhibition of B "# production by exogenous B "# and of the inhibition of propionate and B "# production by oxygen (Quesada-Chanto et al, 1998 ;Vorobjeva, 2000). Methylmalonyl-CoA mutase is a key enzyme in the production of propionic acid (see Vorobjena, 2000, for a review of metabolic pathways in propionibacteria), and a decrease in the enzyme level in the presence of oxygen, by inhibiting synthesis either of the cofactor or of the apoenzyme, would result in decreased propionate levels.…”

Section: Other B 12 Biosynthesis Genesmentioning

confidence: 99%

Isolation and characterization of 14 additional genes specifying the anaerobic biosynthesis of cobalamin (vitamin B12) in Propionibacterium freudenreichii (P. shermanii) The GenBank accession numbers for the sequences reported in this paper are AY033235, AY033236, U13043 and U51164.

et al. 2002

View full text Add to dashboard Cite

A search for genes encoding enzymes involved in cobalamin (vitamin B 12 ) production in the commercially important organism Propionibacterium freudenreichii (P. shermanii) has resulted in the isolation of an additional 14 genes encoding enzymes responsible for 17 steps of the anaerobic B 12 pathway in this organism. All of the genes believed to be necessary for the biosynthesis of adenosylcobinamide from uroporphyrinogen III have now been isolated except two (cbiA and an as yet unidentified gene encoding cobalt reductase). Most of the genes are contained in two divergent operons, one of which, in turn, is closely linked to the operon encoding the B 12 -dependent enzyme methylmalonyl-CoA mutase. The close linkage of the three genes encoding the subunits of transcarboxylase to the hemYHBXRL gene cluster is reported. The functions of the P. freudenreichii B 12 pathway genes are discussed, and a mechanism for the regulation of cobalamin and propionic acid production by oxygen in this organism is proposed.

show abstract

“…Members of the genus Propionibacterium have been used industrially for the production of cheeses, vitamin B 12 (cyanocobalamin), and propionic acid (29). In efforts to clarify details of the biosynthesis of cobalamin and tetrapyrrole derivatives in Propionibacterium, several genes for enzymes involved in these cobalamin biosynthetic pathways have been identified (5,20,28).…”

mentioning

confidence: 99%

Effects of Expression of hemA and hemB Genes on Production of Porphyrin in Propionibacterium freudenreichii

Piao

Kiatpapan

Yamashita

et al. 2004

Appl Environ Microbiol

View full text Add to dashboard Cite

The genus Propionibacterium has a wide range of probiotic activities that are exploited in dairy and fermentation systems such as cheeses, propionic acid, and tetrapyrrole compounds. In order to improve production of tetrapyrrole compounds, we expressed the hemA gene, which encodes ␦-aminolevulinic acid (ALA) synthase from Rhodobacter sphaeroides, and the hemB gene, which encodes porphobilinogen (PBG) synthase from Propionibacterium freudenreichii subsp. shermanii IFO12424, either monocistronically or polycistronically in strain IFO12426. The recombinant strains accumulated larger amounts of ALA and PBG, with resultant 28-to 33-fold-higher production of porphyrinogens, such as uroporphyrinogen and coproporphyrinogen, than those observed in strain IFO12426, which harbored the shuttle vector pPK705.

show abstract

Propionibacteria

Cited by 41 publications

References 0 publications

Characterization of pRGO1, a Plasmid from Propionibacterium acidipropionici , and Its Use for Development of a Host-Vector System in Propionibacteria

Characterization of pRGO1, a Plasmid from Propionibacterium acidipropionici , and Its Use for Development of a Host-Vector System in Propionibacteria

Isolation and characterization of 14 additional genes specifying the anaerobic biosynthesis of cobalamin (vitamin B12) in Propionibacterium freudenreichii (P. shermanii) The GenBank accession numbers for the sequences reported in this paper are AY033235, AY033236, U13043 and U51164.

Effects of Expression of hemA and hemB Genes on Production of Porphyrin in Propionibacterium freudenreichii

Contact Info

Product

Resources

About