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  • 1
    Electronic Resource
    Electronic Resource
    Peroxisome deficiency represses the expression of n-alkane-inducible YlALK1 encoding cytochrome P450ALK1 in Yarrowia lipolytica (2002)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 214 (2002), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Among the eight genes (YlALK1–YlALK8) encoding P450 cytochromes of the CYP52 family of the n-alkane-assimilating yeast Yarrowia lipolytica, Y1ALK1 is most highly induced by n-alkanes with short hydrocarbon chains, such as n-decane, and involved in the initial hydroxylation of n-alkane. To determine the factors regulating YlALK1 expression, we isolated an n-decane assimilation-deficient mutant, B0-6-1, whose YlALK1 expression level was lower than that of the wild-type. By complementation of the mutation of B0-6-1, we cloned a gene having an open reading frame of 1062 bp. The putative gene product is a protein of 354 amino acids and has significant homology to Pex10ps of other organisms. We named this gene YlPEX10. YlPex10p has a C3HC4 ring finger motif common among Pex10ps in its C-terminal region. This motif was also essential for the function of YlPex10p. Both B0-6–1 and a null mutant of YlPEX10 failed to form peroxisome and showed low-level transcription of YlALK1 after the change of carbon source to n-decane. Furthermore, YlPEX5 and YlPEX6 disruptants also showed low-level transcription of YlALK1 like the YlPEX10 disruptant and B0-6–1 mutant. We propose that in this organism peroxisome deficiency represses the expression of n-alkane-inducible YlALK1 encoding cytochrome P450ALK1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2002.tb11321.x
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  • 2
    Electronic Resource
    Electronic Resource
    Isolation of csm1 encoding a class V chitin synthase with a myosin motor-like domain from the rice blast fungus, Pyricularia oryzae (1999)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 170 (1999), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: A gene encoding a chitin synthase with a myosin motor-like domain (csm1) was isolated from Pyricularia oryzae using a PCR fragment amplified from a fungal chitin synthase conserved region. The deduced amino acid sequence of csm1 is homologous to that of CsmA of Aspergillus nidulans (65% identity). The putative gene product of csm1 is consisted of the myosin motor-like domain and a chitin synthase domain as in A. nidulans csmA. The chitin synthase domain of its C-terminus was also homologous to Aspergillus fumigatus ChsE (61.4% identity) and Ustilago maydis Chs6 (48.6% identity) that encode class V chitin synthases. Northern analysis demonstrated that the csm1 was expressed throughout the mycelial growth of P. oryzae. This is the first report on the isolation of the gene encoding a class V chitin synthase with the myosin motor-like domain from P. oryzae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13365.x
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular cloning of a phospholipase D gene from Aspergillus nidulans and characterization of its deletion mutants (2003)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 224 (2003), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We cloned a gene pldA encoding a protein containing phospholipase D (PLD) motifs from a filamentous fungus Aspergillus nidulans. The deduced protein product of pldA consists of 833 amino acids and contains four conserved regions of a PLD gene family. Deletion mutants of pldA grew and formed conidia in a normal manner. Although PLD and transphosphatidylation activities against phosphatidylcholine of the mutant cell extract did not change, the Ca2+-dependent PLD activity against phosphatidylethanolamine was significantly reduced, but not in the wild-type cell extract. This activity was markedly enhanced by high osmotic growth conditions in the wild-type cells, and pldA of A. nidulans likely encodes a Ca2+-dependent phosphatidylethanolamine-hydrolyzing PLD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0378-1097(03)00440-3
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  • 4
    Electronic Resource
    Electronic Resource
    Isolation of a class IV chitin synthase gene from a zygomycete fungus, Rhizopus oligosporus (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 169 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: We found the presence of DNA sequence which shows sequence similarity to the class IV chitin synthase gene (CHS3) of Saccharomyces cerevisiae in the genome of 14 Rhizopus species which belong to zygomycetes. We cloned a gene (chs3), which might correspond to one of these homologous sequences, from Rhizopus oligosporus by low stringency plaque hybridization probed with CHS3. The deduced amino acid sequence of this gene showed highest similarity to the class IV chitin synthase of Neurospora crassa (46.7% identity over 1087 amino acids), showing that this gene encodes a class IV chitin synthase. Northern analysis revealed the differential expression pattern of this gene in the asexual life cycle with highest expression in the early stage of asexual spore formation. This is the first report of the isolation and analysis of a class IV chitin synthase gene from zygomycete fungi.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13291.x
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  • 5
    Electronic Resource
    Electronic Resource
    Cloning of the C-URA3 gene and construction of a triple auxotroph (his5, ade1, ura3) as a useful host for the genetic engineering of Candida maltosa (1993)
    Springer
    Current genetics 23 (1993), S. 205-210 
    Details
    ISSN: 1432-0983
    Keywords: Candida maltosa ; C-URA3 ; Triple auxotroph ; Gene disruption
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The C-URA3 gene of the n-alkane assimilating-yeast Candida maltosa was cloned by complementation of the ura3 mutation of Saccharomyces cerevisiae. The nucleotide sequence of C-URA3 and its deduced amino-acid sequence showed significant homology to those of the orotidine 5′-phosphate decarboxylases of other fungal species. To construct a useful host for genetic engineering of C. maltosa using C-URA3 as a marker, one allele of C-URA3 in a double auxotroph (his5, ade1) was disrupted by C-ADE1, and subsequently two kinds of ura3 mutants were isolated by selecting for spontaneous 5-fluoro-orotic acid (5FOA) resistance. One of the mutants was homozygous for the disruption (ura3::C-ADE1/ura3::C-ADE1); the other was heterozygous (ura3::C-ADE1/ura3). The ura3::C-ADE1 allele in the latter strain was re-substituted by C-URA3 to rescue the adenine auxotroph (his5, ade1, C-URA3/ura3). Finally, by selecting a 5FOA-resistant mutant, a triple auxotroph (his5, ade1, ura3/ura3) was isolated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351497
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  • 6
    Electronic Resource
    Electronic Resource
    Expression of an endogenous and a heterologous gene in Candida maltosa by using a promoter of a newly-isolated phosphoglycerate kinase (PGK) gene (1994)
    Springer
    Current genetics 25 (1994), S. 412-417 
    Details
    ISSN: 1432-0983
    Keywords: Candida maltosa ; PGK ; Expression vector
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A gene encoding phosphoglycerate kinase (PGK) was isolated from the genomic library of C. maltosa to construct an expression vector for this yeast. The PGK gene had an open reading frame of 1251 base pairs encoding approximately 47-kDA polypeptide of 417 amino-acid residues. Expression of this gene assayed by Northern-blot analysis was significantly induced in cells grown on glucose but not in cells grown on n-tetradecane, n-tetradecanol, or oleic acid. By using the promoter region of this gene, an expression vector (termed pMEA1) for C. maltosa was constructed and expression of an endogenous gene (P450alkl encoding one of cytochrome P450s for n-alkane hydroxylation in C. maltosa) and a heterologous gene (LAC4 encoding Kluyveromyces lactis β-galactosidase) was tested. Expression of P450alkl gene was confirmed at both mRNA and protein levels. LAC4 gene expression was confirmed by determining β-galactosidase activity. The activity in cells grown on various carbon sources correlated very well with the expression levels of PGK mRNA in these cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351779
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  • 7
    Electronic Resource
    Electronic Resource
    The Aspergillus nidulans genes chsA and chsD encode chitin synthases which have redundant functions in conidia formation (1997)
    Springer
    Molecular genetics and genomics 253 (1997), S. 520-528 
    Details
    ISSN: 1617-4623
    Keywords: Key words Chitin synthase ; Multigene family ; Cell wall ; Conidia ; Aspergillus nidulans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  We previously isolated three chitin synthase genes (chsA, chsB, and chsC) from Aspergillus nidulans. In the present work, we describe the isolation and characterization of another chitin synthase gene, named chsD, from A. nidulans. Its deduced amino acid sequence shows 56.7% and 55.9% amino acid identity, respectively, with Cal1 of Saccharomyces cerevisiae and Chs3 of Candida albicans. Disruption of chsD caused no defect in cell growth or morphology during the asexual cycle and caused no decrease in chitin content in hyphae. However, double disruption of chsA and chsD caused a remarkable decrease in the efficiency of conidia formation, while double disruption of chsC and chsD caused no defect. Thus it appears that chsA and chsD serve redundant functions in conidia formation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050353
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  • 8
    Electronic Resource
    Electronic Resource
    Cloning and characterization of two 3-phosphoglycerate kinase genes of Rhizopus niveus and heterologous gene expression using their promoters (1994)
    Springer
    Current genetics 25 (1994), S. 524-530 
    Details
    ISSN: 1432-0983
    Keywords: Rhizopus niveus ; 3-Phosphoglycerate kinase ; β-Glucuronidase (uidA) ; Gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two 3-phosphoglycerate kinase genes (pgk1 and pgk2) were cloned from Rhizopus niveus. It was deduced that both pgk genes have two introns. They have open reading frames of 1355 bp and 1356 bp, and code for proteins of 417 and 416 amino acids, respectively. The first introns of both genes are located at similar positions as those of pgk genes from other fungi based on the deduced amino-acid sequences of PGK proteins. The position of their second introns was similar to that of the seventh intron of the human pgk gene. The deduced amino-acid sequences of PGK proteins show high identity (64.8–72.2%) to those of PGKs of other filamentous fungi. When the promoters of each of the pgk genes were fused to the E. coli β-glucuronidase (GUS) gene and introduced into R. niveus, significant GUS activities were detected in the cell lysates of the transformants, suggesting that GUS protein was expressed under the control of both pgk gene promoters in R. niveus. GUS activity was induced by glucose but not by glycerol, indicating that expression of R. niveus pgk genes was regulated by the carbon source.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351673
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  • 9
    Electronic Resource
    Electronic Resource
    Molecular diversity of three S-allele cDNAs associated with gametophytic self-incompatibility in Lycopersicon peruvianum (1994)
    Springer
    Plant molecular biology 26 (1994), S. 757-762 
    Details
    ISSN: 1573-5028
    Keywords: cDNA ; gametophytic self-incompatibility ; Lycopersicon peruvianum ; polymerase chain reaction (PCR) ; ribonuclease activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We isolated S allele-associated cDNA clones from each of the stylar cDNA libraries of Lycopersicon peruvianum of two different S genotypes (S 12Sband S 13 S c) with S 11 S callele-associated cDNA (LPS11) as a probe. The longest cDNA clones, designated LPS12 and LPS13, which were 779 bp and 853 bp in length, contained open reading frames of 189 and 210 amino acids, respectively. The three S alleleassociated cDNAs (LPS11, LPS12, and LPS13) did not cross-hybridize to each other under highly stringent condition by northern blot analysis. Their average identity to Nicotiana alata S-proteins so far was 49%. The fragments corresponding to LPS11 or LPS12 cosegregated with their respective S alleles in genetic crosses. From these results, we conclude that the three cloned cDNAs were derived from the three different S alleles of L. peruvianum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00013760
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  • 10
    Electronic Resource
    Electronic Resource
    Cloning of the chitin synthase 3 gene from Candida albicans and its expression during yeast-hyphal transition (1993)
    Springer
    Molecular genetics and genomics 241 (1993), S. 351-358 
    Details
    ISSN: 1617-4623
    Keywords: Candida albicans ; Chitin synthase ; Nucleotide sequence ; Morphogenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The chitin synthase 3 gene (CACHS3) has been cloned from Candida albicans. The yeast CAL1 gene encoding the chitin synthase 3 of Saccharomyces cerevisiae was used as a probe for the isolation of the gene from C. albicans. The CAL1 homolog was identified in Southern blots of C. albicans genomic DNA and cloned from a C. albicans genomic DNA library. The nucleotide sequences of two partial clones were determined and combined giving a total length of 4610 bp. A continuous open reading frame of 3525 by encoding a predicted protein of 1175 amino acids and molecular mass of 131 850 daltons was identified. A comparison of the deduced amino acid sequences of CAL1 and the Candida chitin synthase 3 protein showed 59.3% identitiy. Southern blot analysis indicates that the CACHS3 gene is present in a single copy in the genome and maps to chromosome I. Northern blot analysis shows that expression of chitin synthase 3 gene is dramatically increased during the transition from the yeast to the hyphal form of C. albicans. This change in transcription level strongly suggests that CACHS3 may play a role in Candida morphogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00284688
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