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  • 1
    Electronic Resource
    Electronic Resource
    Development of an integrative DNA transformation system for the yeast Candida utilis (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 165 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We report here the development of an auxotrophic transformation system for the food yeast Candida utilis. To facilitate molecular studies in Candida utilis, we isolated auxotrophic strains for uracil biosynthesis by the combination of NTG-mutagenesis and 5-fluorotic acid (FOA) selection. The ura− mutation could be functionally complemented by the homologous URA3 gene. We used both, LiAc and electroporation methods to direct insertions at the ura3 locus through homologous recombination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13166.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of a dextranase-encoding cDNA from Penicillium minioluteum (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 143 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A cDNA from Penicillium minioluteum HI-4 encoding a dextranase (1,6-α-glucan hydrolase, EC 3.2.1.11) was isolated and characterized. cDNA clones corresponding to genes expressed in dextran-induced cultures were identified by differential hybridization. Southern hybridization and restriction mapping analysis of selected clones revealed four different groups of cDNAs. The dextranase cDNA was identified after expressing a cDNA fragment from each of the isolated groups of cDNA clones in the Escherichia coli T7 system. The expression of a 2 kb cDNA fragment in E. coli led to the production of a 67 kDa protein which was recognized by an anti-dextranase polyclonal antibody. The cDNA contains 2109 bp plus a poly(A) tail, coding for a protein of 608 amino acids, including 20 N-terminal amino acid residues which might correspond to a signal peptide. There was 29% sequence identity between the P. minioluteum dextranase and the dextranase from Arthrobacter sp. CB-8.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08477.x
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of mutants as an approach to a transformation system in Kluyveromyces marxianus (1996)
    Springer
    Current genetics 30 (1996), S. 89-92 
    Details
    ISSN: 1432-0983
    Keywords: Keywords Kluyveromyces marxianus ; Yeast ; HIS3 ; Mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A method to obtain K. marxianus mutants has been developed. Different auxotrophic mutants were isolated by nystatin and snail-enzyme enrichment procedures using an incubation time of 2 h before adding the antibiotic or the enzyme respectively. All his mutants analyzed by complementation tests turned out to belong to the same complementation group. Some of them were transformed and complemented by the S. cerevisiae HIS3 gene. These non-reverting his3 mutants contain no heterologous sequence, which is essential to make them acceptable for application in the food industry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050105
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Transformation of Kluyveromyces lactis cells by plasmid DNA does not require alkaline cations (1985)
    Springer
    Biotechnology letters 7 (1985), S. 723-726 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A procedure for the transformation ofKluyveromyces lactis based on the Li salt method for introducing plasmid DNA into intact yeast cells is described. Contrary toSaccharomyces cerevisiae, lithium salts are dispensable for inducing competence inK. lactis. 2-Mercaptoethanol, a compound that stimulates transformation inS. cerevisiae, showed an opposite effect. inK. lactis. On the other hand, the presence of PEG 4000 and a heat shock were absolutely required to obtain high transformation efficiency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01032283
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning of the Penicillium minioluteum gene encoding dextranase and its expression in Pichia pastoris (1996)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 12 (1996), S. 1187-1200 
    Details
    ISSN: 0749-503X
    Keywords: dextranase ; Penicillium minioluteum ; Pichia pastoris ; heterologous gene expression ; protein secretion ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The DEX gene encoding an extracellular dextranase was isolated from the genomic DNA library of Penicillium minioluteum by hybridization using the dextranase cDNA as a probe. Comparison of the gene and cDNA sequences revealed that the DEX gene does not contain introns. Amino acid sequences comparison of P. minioluteum dextranase with other reported dextranases reveals a significant homology (29% identity) with a dextranase from Arthrobacter sp. CB-8. The DEX gene fragment encoding a mature protein of 574 amino acids was expressed in the methylotrophic yeast Pichia pastoris by using the SUC2 gene signal sequence from Saccharomyces cerevisiae under control of the alcohol oxidase-1 (AOX1) promoter. Over 3·2g/l of enzymatically active dextranase was secreted into the medium after induction by methanol. The yeast product was indistinguishable from the native enzyme in specific activity and the N-terminus of both proteins were identical.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 6
    Electronic Resource
    Electronic Resource
    Isolation of the Pichia pastoris PYC1 gene encoding pyruvate carboxylase and identification of a suppressor of the pyc phenotype (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 647-654 
    Details
    ISSN: 0749-503X
    Keywords: anaplerotic reactions ; glyoxylate cycle ; catabolite repression ; Pichia ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have cloned and characterized a gene encoding pyruvate carboxylase from the methylotrophic yeast Pichia pastoris. Disruption of this gene produced inability to grow in minimal medium with glucose as carbon source and ammonium as nitrogen source. Growth was possible with aspartate or glutamate as nitrogen source. The gene PpPYC1 expressd from its own promoter was able to rescue the phenotype of Saccharomyces cerevisiae mutants devoid of pyruvate carboxylase.In a P. pastoris strain carrying a disrupted PpPYC1 gene we have isolated spontaneous mutants able to grow in non-permissive conditions. In a mutant strain grown in glucose several enzymes sensitive to catabolite repression were derepressed. The strain also had elevated levels of glutamate dehydrogenase (NAD) both in repressed and derepressed conditions. The sequence of the PpPYC1 gene has been entered in the EMBL nucleotide sequence databank: Accession Number Y11106. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
  • 7
    Electronic Resource
    Electronic Resource
    Cloning and sequence analysis of the gene encoding invertase (INV1) from the yeast Candida utilis (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 1223-1232 
    Details
    ISSN: 0749-503X
    Keywords: Candida utilis ; β-fructofuranosidase ; glycosyl hydrolase ; signal peptide ; sucrose ; polymerase chain reaction ; invertase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The gene INV1 encoding invertase from the yeast Candida utilis has been cloned using a homologous PCR hybridization probe, amplified with two sets of degenerate primers designed considering sequence comparisons between yeast invertases. The cloned gene was sequenced and found to encode a polypeptide of 533 amino acids that contain a 26 amino-acid signal peptide and 12 potential N-glycosylation sites. The nucleotide sequences of the 5′ and 3′ non-coding regions were found to contain motifs probably involved in initiation, regulation and termination of gene transcription. The amino-acid sequence shows significant identity with other yeast, bacterial and plant β-fructofuranosidases. The INV1 gene from C. utilis was able to complement functionally the suc2 mutation of S. cerevisiae. The sequence presented here has been deposited in the EMBL data library under Accession Number Y12659. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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    Paper (German National Licenses)
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