Secretion of Aspergillus oryzae alkaline protease in an osmophilic yeast, Zygosaccharomyces rouxii.

Ogawa, Yoshiaki; Tatsumi, Hiroki; Murakami, Seiji; Ishida, Yutaka; Murakami, Kohji; Masaki, Atsushi; Kawabe, Haruhide; Arimura, Hirofumi; Nakano, E.; Motai, Hiroshi; Toh‐e, Akio

doi:10.1271/bbb1961.54.2521

Cited by 24 publications

(15 citation statements)

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“…Expression of the hly gene was first tried in an osmophilic yeast, Zygosaccharomyces rouxii (19), in media containing 18% NaCI; however, plasmid vectors containing hly were quite unstable, and thus no expressions was observed.…”

Section: R S H L Q N T a V D V G L S S E E Q G H G R V D 1 10o1 Tcamentioning

confidence: 99%

Molecular cloning and sequencing of the gene for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii

et al. 1992

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The gene of a halophilic alkaline serine protease, halolysin, from an unidentified halophilic archaea (archaebacterium) was cloned and its nucleotide sequence was determined. The deduced amino acid sequence showed that halolysin consists of 411 amino acids, with a molecular weight of 41,963. The highest homology was found with thermitase from Thermoactinomyces vulgaris. Halolysin has a long C-terminal extension of approximately 120 amino acids which has not been found in other extracellular subtilisin type serine proteases. The gene, hly, was expressed in another halophilic archaea, Haloferax volcanii, in a medium containing 18% salts by using a plasmid shuttle vector which has a novobiocin resistance determinant as a selectable marker.

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Section: R S H L Q N T a V D V G L S S E E Q G H G R V D 1 10o1 Tcamentioning

confidence: 99%

Molecular cloning and sequencing of the gene for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii

et al. 1992

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“…pCXJ-kanl contains the entire pKDl sequence (see Methods). The stability of transformants as defined in Table 1 kul et al., 1987a;Ogawa et al, 1990). These sites are in an intergenic region of the plasmid.…”

Section: Curing Of Pkwl From K Waltiimentioning

confidence: 99%

Characterization of a circular plasmid from the yeast Kluyveromyces waltii

Chen

Cong

Wésolowski-Louvel

et al. 1992

Journal of General Microbiology

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A new plasmid was found in the yeast Kluyoeromyces wdtii. This high-copy-number plasmid, named pKW1, is a double-stranded circular DNA plasmid of 5619 bp. It has several features characteristic of the 2ptype plasmids: presence of two inverted repeats and four open reading frames, as well as the interconversion of two isomeric forms. However, the nucleotide sequence shows little homology with known yeast plasmids. An ARS function was localized within a segment of 545 bp near one of the inverted repeats. Chimeric plasmids carrying this segment efficiently transformed K. wdtii. A strain of K. waltii cured of the plasmid (ciro) was also obtained. In the pKWl sequence, a functionally neutral region was found at which foreign DNA can be inserted with little effect on plasmid stability. Such constructions carrying the full sequence of pKWl replicated autonomously in a cir" host and were particularly stable. pK W 1-derived full-sequence plasmids also transformed K. thermotolerans, but not K. lactis.

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“…Indeed, fed-batch fermentations are required to attain high cell densities of S. cerevisiae [2,3]. While expression and secretion of heterologous proteins has been achieved in Z. rouxii [30], up to now no comparable studies have been presented for Z. bailii. Prominent examples are Hansenula polymorpha [4,5], Pichia pastoris [6,7], Kluyveromyces lactis [8,9] and Yarrowia lipolytica [10,11], among others.…”

Section: Introductionmentioning

confidence: 99%

The yeast : a new host for heterologous protein production, secretion and for metabolic engineering applications

Branduardi

Valli

Brambilla

et al. 2004

FEMS Yeast Research

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Molecular tools for the production of heterologous proteins and metabolic engineering applications of the non-conventional yeast Zygosaccharomyces bailii were developed. The combination of Z. bailii's resistance to relatively high temperature, osmotic pressure and low pH values, with a high specific growth rate renders this yeast potentially interesting for exploitation for biotechnological purposes as well as for the understanding of the biological phenomena and mechanisms underlying the respective resistances. Looking forward to these potential applications, here we present the tools required for the production and the secretion of different heterologous proteins, and one example of a metabolic engineering application of this non-conventional yeast, employing the newly developed molecular tools.

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Secretion of Aspergillus oryzae alkaline protease in an osmophilic yeast, Zygosaccharomyces rouxii.

Cited by 24 publications

References 1 publication

Molecular cloning and sequencing of the gene for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii

Molecular cloning and sequencing of the gene for a halophilic alkaline serine protease (halolysin) from an unidentified halophilic archaea strain (172P1) and expression of the gene in Haloferax volcanii

Characterization of a circular plasmid from the yeast Kluyveromyces waltii

The yeast : a new host for heterologous protein production, secretion and for metabolic engineering applications

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