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  • 1
    Electronic Resource
    Electronic Resource
    The 3-phosphoglycerate kinase gene of the yeast Yarrowia lipolytica de-represses on gluconeogenic substrates (1996)
    Springer
    Current genetics 29 (1996), S. 446-456 
    Details
    ISSN: 1432-0983
    Keywords: Key words  Yarrowia lipolytica ; 3-Phosphoglycerate kinase ; Expression ; Disruption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract   We have isolated the 3-phosphoglycerate kinase (PGK) gene of the yeast Yarrowia lipolytica by probing a genomic library with a PCR fragment amplified with primers deduced from two highly conserved regions of various PGKs. It is a unique sequence encoding a polypeptide of 417 residues with extensive homology to other PGKs, especially to that of Aspergillus nidulans (76% identity). The expression of the Y. lipolytica PGK1 gene proved to be higher on gluconeogenic substrates than on glycolytic ones. Haploid strains harboring a disrupted allele were able to grow on mixtures of a gluconeogenic carbon source and of a glycolytic one, but required proline supplementation in the presence of glucose, and were inhibited by glycerol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050070
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  • 2
    Electronic Resource
    Electronic Resource
    The 3-phosphoglycerate kinase gene of the yeastYarrowia lipolytica de-represses on gluconeogenic substrates (1996)
    Springer
    Current genetics 29 (1996), S. 446-456 
    Details
    ISSN: 1432-0983
    Keywords: Yarrowia lipolytica ; 3-Phosphoglycerate kinase ; Expression ; Disruption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated the 3-phosphoglycerate kinase (PGK) gene of the yeastYarrowia lipolytica by probing a genomic library with a PCR fragment amplified with primers deduced from two highly conserved regions of various PGKs. It is a unique sequence encoding a polypeptide of 417 residues with extensive homology to other PGKs, especially to that ofAspergillus nidulans (76% identity). The expression of theY. lipolytica PGK1 gene proved to be higher on gluconeogenic substrates than on glycolytic ones. Haploid strains harboring a disrupted allele were able to grow on mixtures of a gluconeogenic carbon source and of a glycolytic one, but required proline supplementation in the presence of glucose, and were inhibited by glycerol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02221513
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  • 3
    Electronic Resource
    Electronic Resource
    Characterisation of HlyC and mechanism of activation and secretion of haemolysin from E. coli 2001
    Amsterdam : Elsevier
    FEBS Letters 187 (1985), S. 339-344 
    Details
    ISSN: 0014-5793
    Keywords: Hemolysin secretion ; Post-translational modification ; hlyC sequence
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(85)81272-2
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  • 4
    Electronic Resource
    Electronic Resource
    The C-terminal, 23 kDa peptide of E. coli haemolysin 2001 contains all the information necessary for its secretion by the haemolysin (Hly) export machinery
    Amsterdam : Elsevier
    FEBS Letters 204 (1986), S. 331-335 
    Details
    ISSN: 0014-5793
    Keywords: (E. coli) Hemolysin C-terminal secretion signal Expression vector Protein
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(86)80838-9
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  • 5
    Electronic Resource
    Electronic Resource
    Stabilization of methionine-rich protein in Saccharomyces cerevisiae: targeting of BZN protein into the peroxisome (1994)
    Springer
    Current genetics 26 (1994), S. 390-397 
    Details
    ISSN: 1432-0983
    Keywords: Overexpression ; Peroxisomes ; Saccharomyces cerevisiae ; Stabilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have constructed a gene coding for the 12-kDa intermediate form of the 2s methionine-rich protein from Bertholletia excelsa seeds. This protein, expressed intracellularly in yeast, is characterised by a 20-min balf-life. By adding 11 amino acids corresponding to the peroxisome-targeting sequence (PTSc) of luciferase, we have significantly increased its half-life. This stabilization allowed accumulation of the BZN protein into the peroxisome as judged by cell fractionation. Accumulation of the 12-kDa protein results in a significant increase of the total methionine content in yeast cells (30%) indicating that such a microorganism could represent a practicable protected shuttl for an animal-feed additive.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309924
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  • 6
    Electronic Resource
    Electronic Resource
    Peroxisomal β-oxidation activities and γ-decalactone production by the yeast Yarrowia lipolytica (1998)
    Springer
    Applied microbiology and biotechnology 49 (1998), S. 295-300 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract γ-Decalactone is a peachy aroma compound resulting from the peroxisomal β-oxidation of ricinoleic acid by yeasts. The expression levels of acyl-CoA oxidase (gene deletion) and 3-ketoacyl-CoA thiolase activities (gene amplification on replicative plasmids) were modified in the yeast Yarrowia lipolytica. The effects of these modifications on β-oxidation were measured. Overexpression of thiolase activity did not have any effect on the overall β-oxidation activity. The disruption of one of the acyl-CoA oxidase genes resulted in an enhanced activity. The enhancement led to an increase of overall β-oxidation activity but reduced the γ-decalactone production rates. This seemed to indicate a non-rate-limiting role for β-oxidation in the biotransformation of ricinoleic acid to γ-decalactone by the yeast Yarrowia lipolytica. All strains produced and then consumed γ-decalactone. We checked the ability of the different strains to consume γ-decalactone in a medium containing the lactone as sole carbon source. The consumption of the strain overexpressing acyl-CoA oxidase activity was higher than that of the wild-type strain. We␣concluded that peroxisomal β-oxidation is certainly involved in γ-decalactone catabolism by the yeast Y.␣lipolytica. The observed production rates probably depend on an equilibrium between production and consumption of the lactone.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051172
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  • 7
    Electronic Resource
    Electronic Resource
    Regulation of haemolysin synthesis in E. coli determined by HLY genes of human origin (1985)
    Springer
    Molecular genetics and genomics 199 (1985), S. 111-116 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have previously reported the secretion of a 107K polypeptide into the medium from a haemolytic E. coli K12 strain (Mackman and Holland 1984a). In addition, we demonstrated that haemolysin production was correlated with the presence of this polypeptide in the growth medium in a large number of E. coli isolates of human and animal origin (Mackman and Holland 1984b). In this paper we confirm that the 107K polypeptide is indeed haemolysin: both haemolytic activity and the 107K polypeptide show a similar pattern of accumulation during the growth cycle; identical levels are produced in three different growth media; they have the same half-life in minimal medium. The results also show that the expression of haemolysin is not influenced by the growth medium or subject to catabolite repression. However, expression is apparently switched off as cells enter the late exponential phase of growth. Finally, we present data indicating that the previously reported variation in haemolysin production in different media is entirely due to the instability of the haemoolysin itself. Degradation of the 107K polypeptide in the medium was accompanied by the accumulation of a major breakdown product of 60K.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327519
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  • 8
    Electronic Resource
    Electronic Resource
    The carboxy-terminal region of haemolysin 2001 is required for secretion of the toxin fromEscherichia coli (1986)
    Springer
    Molecular genetics and genomics 205 (1986), S. 127-133 
    Details
    ISSN: 1617-4623
    Keywords: Haemolysin ; Secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary As a first step in the detailed analysis of the mechanism of secretion of haemolysin, we sought to identify sequences or domains within haemolysin A (HlyA) that are essential for its secretion. For this purpose we examined the properties of a deletion and Tn5 insertions into the region of theHlyA gene encoding the C-terminal part of the protein, since both of these are relatively simple to generate. We showed that removal of 27 amino acids from the C-terminus of HlyA is sufficient to inhibit secretion drastically, although the residual polypeptide is still haemolytically active. Cellular fractionation studies showed that haemolytic activity does not accumulate in large amounts within the periplasmic space during normal secretion. More significantly, activity does not appear to accumulate within this compartment when the export functionshlyB andhlyD are removed. These results are consistent with a mechanism in which interaction of the C-terminus of HlyA with the secretion machinery, located in the inner membrane, is followed by direct transfer of haemolysin to the medium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02428042
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  • 9
    Electronic Resource
    Electronic Resource
    Genetical and functional organisation of the Escherichia coli haemolysin determinant 2001 (1985)
    Springer
    Molecular genetics and genomics 201 (1985), S. 282-288 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have identified gene products corresponding to hlyC, hlyA and hlyD encoded by the Escherichia coli haemolytic determinant 2001 of human origin cloned into the recombinant plasmid pLG570. The product of hlyC is required for the “activation” of the inactive 107K polypeptide encoded by the hlyA gene. the activated 107K protein constitutes the active haemolysin secreted into the medium. hlyB and hlyD are separate regions defined by complementation studies and encode functions essential for the export of haemolysin with hlyD encoding a 53K protein. Complementation studies using subclones and Tn5 insertions into pLG570 have revealed the presence of two major promoters upstream of hlyC and hlyD which transcribe the four hly genes in the same direction. Finally, we were able to reconstitute the complete haemolysin system from three different plasmids encoding hlyC, hlyA and hlyB+hlyD, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425672
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  • 10
    Electronic Resource
    Electronic Resource
    Identification of polypeptides required for the export of haemolysin 2001 from E. coli (1985)
    Springer
    Molecular genetics and genomics 201 (1985), S. 529-536 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have identified the polypeptides encoded by the haemolysin export genes from a haemolytic determinant 2001 carried by pLG570. This was previously cloned from an E. coli strain, serotype 04 isolated from a human urinary tract infection. Subclones from the recombinant plasmid pLG570 carrying hlyD analysed in vitro and in minicells showed that this gene is transcribed from an independent promoter and encodes a 53 Kd polypeptide. In contrast, detectable levels of the gene products encoded by hlyB were only observed when transcription presumably emanated from a vector promoter. This gene was found to encode at least two polypeptides apparently expressed from alternative translational start sites within a single reading frame. In minicells the major product was a 66 Kd polypeptide whilst after expression in nitro the major product was a 46 Kd polypeptide. Transposon mutagenesis leading to the synthesis of the expected truncated polypeptides was used to confirm the identity of the hlyD and the two hlyB products. Preliminary results suggest that the majority of the 53 Kd polypeptide is located in the inner membrane when cell envelopes from minicells and maxicells were fractionated using sarkosyl, although residual amounts of the 53 Kd polypeptide were also found in the outer membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331351
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