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  • 1
    Electronic Resource
    Electronic Resource
    Kinetics and mechanisms of the substitution reactions of cobalt dithiolate systems (1971)
    s.l. : American Chemical Society
    Inorganic chemistry 10 (1971), S. 196-198 
    Details
    ISSN: 1520-510X
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/ic50095a037
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of theugatA gene ofUstilago maydis, isolated by homology to thegatA gene ofAspergillus nidulans (1996)
    Springer
    Current genetics 29 (1996), S. 360-369 
    Details
    ISSN: 1432-0983
    Keywords: Ustilago maydis ; GABA aminotransferase ; Heterologous expression ; Sequence conservation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A gene encoding a putative GABA aminotransferase (ugatA) was isolated from the basidiomyceteUstilago maydis via heterologous hybridization to the GABA aminotransferase gene (gatA) ofAspergillus nidulans. The derived amino-acid sequence ofugatA shows strong identity throughout the protein to the GABA aminotransferase enzymes fromA. nidulans andSaccharomyces cerevisiae. Northern analysis inU. maydis indicated that theugatA transcript is inducible by the ω-amino acids GABA and β-alanine, and is not subject to nitrogen catabolite repression. With the use ofugatA promoter-lacZ fusion constructs, it was demonstrated that the removal of sequences located approximately 250 by 5′ to the translational start site ofugatA (including multiple copies of a 7-bp direct repeat) resulted in the loss of induction by ω-amino acids. While theugatA gene under the control of theA. nidulans gatA promoter was able to fully complement agatA − phenotype inA. nidulans, the full-lengthugatA gene was not, suggesting a lack of expression from theU. maydis promoter inA. nidulans. AU. maydis strain with a gene disruption at theugatA locus showed decreased growth on β-alanine as a sole nitrogen source, but was able to grow on GABA as a sole nitrogen source, indicating an alternative pathway for the utilization of GABA inU. maydis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02208617
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the ugatA gene of Ustilago maydis, isolated by homology to the gatA gene of Aspergillus nidulans (1996)
    Springer
    Current genetics 29 (1996), S. 360-369 
    Details
    ISSN: 1432-0983
    Keywords: Key words Ustilago maydis ; GABA aminotransferase ; Heterologous expression ; Sequence conservation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  A gene encoding a putative GABA aminotransferase (ugatA) was isolated from the basidiomycete Ustilago maydis via heterologous hybridization to the GABA aminotransferase gene (gatA) of Aspergillus nidulans . The derived amino-acid sequence of ugatA shows strong identity throughout the protein to the GABA aminotransferase enzymes from A. nidulans and Saccharomyces cerevisiae. Northern analysis in U. maydis indicated that the ugatA transcript is inducible by the ω-amino acids GABA and β-alanine, and is not subject to nitrogen catabolite repression. With the use of ugatA promoter-lacZ fusion constructs, it was demonstrated that the removal of sequences located approximately 250 bp 5′ to the translational start site of ugatA (including multiple copies of a 7-bp direct repeat) resulted in the loss of induction by ω-amino acids. While the ugatA gene under the control of the A. nidulans gatA promoter was able to fully complement a gatA - phenotype in A. nidulans, the full-length ugatA gene was not, suggesting a lack of expression from the U. maydis promoter in A. nidulans. A U. maydis strain with a gene disruption at the ugatA locus showed decreased growth on β-alanine as a sole nitrogen source, but was able to grow on GABA as a sole nitrogen source, indicating an alternative pathway for the utilization of GABA in U. maydis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050057
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  • 4
    Electronic Resource
    Electronic Resource
    The Aspergillus nidulans gltA gene encoding glutamate synthase is required for ammonium assimilation in the absence of NADP-glutamate dehydrogenase (1999)
    Springer
    Current genetics 34 (1999), S. 467-471 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsAspergillus nidulans ; Ammonium assimilation ; Glutamate synthase ; Gene inactivation ; Glutamate dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutants of Aspergillus nidulans lacking NADP-glutamate dehydrogenase activity grow more poorly than wild-type strains on ammonium as a sole nitrogen source. The leaky growth of these mutants is indicative of an alternative pathway of ammonium assimilation and glutamate biosynthesis. We have PCR-amplified a portion of the A. nidulans gene encoding glutamate synthase and used this sequence to inactivate the genomic copy. This gene, designated gltA, was found to be dispensable for growth on ammonium in the presence of NADP-glutamate dehydrogenase activity. However, a strain carrying the gltA inactivation together with an NADP-glutamate dehydrogenase structural gene mutation (gdhA) was unable to grow on ammonium or on nitrogen sources metabolized via ammonium. The gltA gene was located to linkage group V of the A. nidulans genetic map.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050421
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  • 5
    Electronic Resource
    Electronic Resource
    An Aspergillus oryzae CCAAT-binding protein, AoCP, is involved in the high-level expression of the Taka-amylase A gene (2000)
    Springer
    Current genetics 37 (2000), S. 380-387 
    Details
    ISSN: 1432-0983
    Keywords: Key wordsAspergillus oryzae ; Nuclear protein ; CCAAT-box binding protein ; HAPC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Aspergillus oryzae contains a nuclear protein designated AoCP, which binds specifically to a CCAAT sequence in the promoter region of the A. oryzae Taka-amylase A gene. A gene encoding a homologue of Aspergillus nidulans HAPC, a subunit of the A. nidulans CCAAT binding complex, was isolated from A. oryzae and designated AohapC. AoHAPC comprises 215 amino acids and shows 84% identity to A. nidulans HAPC. Transformation of the A. nidulans hapC deletion strain with the AohapC gene restored the CCAAT binding activity, resulting in both enhancement of taa gene expression and complementation for the poor growth phenotype of this strain. Furthermore, introduction of the AohapC gene also restored the expression of the A. nidulans eglA gene, encoding an endo-β-1,4-glucanase, in the deletion strain. These results indicate functional interchangeability of the genes from two species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940000125
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  • 6
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    Unknown
    The Church of Ireland. (1935)
    Washington : Periodicals Archive Online (PAO)
    Catholic historical review. 21 (1935/1936) 400 
    Details
    ISSN: 0008-8080
    Topics: History , Theology and Religious Studies
    URL: http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&res_dat=xri:pao:&rft_dat=xri:pao:article:1053-1935-021-00-000011
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  • 7
    Electronic Resource
    Electronic Resource
    The positively acting amdA gene of Aspergillus nidulans encodes a protein with two C2H2 zinc-finger motifs (1995)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 15 (1995), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Semi-dominant mutations in the amdA gene iead to elevated expression of the gene encoding acetamidase, amdS. These mutations also cause constitutive expression of the acetate-inducible gene, aciA. In the amdS 5′ regulatory region, two cis-acting mutations, amd166 anti amd1666, have been isolated which specifically affect amdA activation of amdS. These mutations are a duplication and a triplication of an 18bp GA-rich sequence, thought to define the amdA site of action within the amdS promoter region. Similar GA-rich sequences have also been found in the 5′ region of aciA. This paper describes the cloning and initial functional characterization of the amdA gene and two of its mutant alleles. The wild-type amdA gene has been cloned by a chromosome walk from genes gatA and alcC on linkage group VII and localized by complementation of an amdA loss-of-function mutation. Transcriptional analysis reveals that the gene is expressed constitutively at low levels under growth conditions which affect expression of amdS and aciA. The gene is predicted to encode an 880-amino-acid protein which contains two C2H2 zinc fingers, a nuclear localization sequence and two transcriptional activation domains. The amdA7 semi-dominant gain-of-function mutation results in a glycine to aspartate substitution which would increase the acidity of one of these regions. Analysis of in vitro generated mutations in the 5′ region of amdS using an amdS::lacZ reporter has been used to localize the site of action of AmdA. The C2H2 zinc-finger motifs identified in the protein are similar to those found in the carbon catabolite repressor protein, CreA, which also regulates amdS and recognizes sequences which overlap with the proposed site of action for AmdA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1995.tb02365.x
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  • 8
    Electronic Resource
    Electronic Resource
    The Ras and Rho GTPases genetically interact to co-ordinately regulate cell polarity during development in Penicillium marneffei (2005)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 55 (2005), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Ras and Rho GTPases have been examined in a wide variety of eukaryotes and play varied and often overlapping roles in cell polarization and development. Studies in Saccharomyces cerevisiae and mammalian cells have defined some of the central activities of these GTPases. However, these paradigms do not explain the role of these proteins in all eukaryotes. Unlike yeast, but like more complex eukaryotes, filamentous fungi have Rac-like proteins in addition to Ras and Cdc42. To investigate the unique functions of these proteins and determine how they interact to co-ordinately regulate morphogenesis during growth and development we undertook a genetic analysis of GTPase function by generating double mutants of the Rho GTPases cflA and cflB and the newly isolated Ras GTPase rasA from the dimorphic pathogenic fungus, Penicillium marneffei. P. marneffei growth at 25°C is as multinucleate, septate, branched hyphae which are capable of undergoing asexual development (conidiation), while at 37°C, uninucleate pathogenic yeast cells which divide by fission are produced. Here we show that RasA (Ras) acts upstream of CflA (Cdc42) to regulate germination of spores and polarized growth of both hyphal and yeast cells, while also exhibiting CflA-independent activities. CflA (Cdc42) and CflB (Rac) co-ordinately control hyphal cell polarization despite also having unique roles in regulating conidial germination and polarized growth of yeast cells (CflA) and polarized growth of conidiophore cell types and hyphal branching (CflB).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2005.04485.x
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  • 9
    Electronic Resource
    Electronic Resource
    TupA, the Penicillium marneffei Tup1p homologue, represses both yeast and spore development (2003)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 48 (2003), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Fungal pathogenesis is frequently associated with dimorphism – morphological changes between yeast and filamentous forms. Penicillium marneffei, an opportunistic human pathogen, exhibits temperature-dependent dimorphism, with growth at 25°C as filamentous multinucleate hyphae switching at 37°C to uninucleate yeast cells associated with intracellular pathogenesis. The filamentous hyphae also undergo asexual development generating uninucleate spores, the infectious propagules. Both processes require a switch to coupled nuclear and cell division. Homologous regulators, including Tup1p/GROUCHO-related WD40 repeat transcription factors, control dimorphism in Candida albicans and asexual development in Aspergillus nidulans. Unlike these fungi, P. marneffei has both developmental programmes allowing examination of common and programme-specific controls. We show that deletion of tupA, the P. marneffei TUP1 homologue, confers reduced filamentation and inappropriate yeast morphogenesis at 25°C, in stark contrast to constitutive filamentation observed when C. albicans TUP1 is deleted. Deletion of tupA also confers premature brlA-dependent asexual development, unlike reduced asexual development in the corresponding A. nidulans rcoA deletion mutant. Furthermore, the A. nidulans rcoA deletion mutant is self-sterile, and we show that tupA from P. marneffei, which lacks an apparent sexual cycle, complements both the asexual and sexual development phenotypes. Therefore, TupA coordinates cell fate by promoting filamentation and repressing both spore and yeast morphogenetic programmes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2003.03426.x
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  • 10
    Electronic Resource
    Electronic Resource
    The abaA homologue of Penicillium marneffei participates in two developmental programmes: conidiation and dimorphic growth (2000)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 38 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Penicillium marneffei is the only known species of its genus that is dimorphic. At 25°C, P. marneffei exhibits true filamentous growth and undergoes asexual development producing spores borne on complex structures called conidiophores. At 37°C, P. marneffei undergoes a dimorphic transition to produce uninucleate yeast cells that divide by fission. We have cloned a homologue of the Aspergillus nidulans abaA gene encoding an ATTS/TEA DNA-binding domain transcriptional regulator and shown that it is involved in both these developmental programs. Targeted deletion of abaA blocks asexual development at 25°C before spore production, resulting in aberrant conidiophores with reiterated terminal cells. At 37°C, the abaA deletion strain fails to switch correctly from multinucleate filamentous to uninucleate yeast cells. Both the transitional hyphal cells, which produce the yeast cells, and the yeast cells themselves contain multiple nuclei. Expression of the abaA gene is activated during both conidiation and the hyphal–yeast switch. Interestingly, the abaA gene of the filamentous monomorphic fungus A. nidulans can complement both conidiation and dimorphic switching defects in the P. marneffei abaA mutant. In addition, ectopic overexpression of abaA results in anucleate yeast cells and multinucleate vegetative filamentous cells. These data suggest that abaA regulates cell cycle events and morphogenesis in two distinct developmental programmes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.02202.x
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