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  • 1
    Electronic Resource
    Electronic Resource
    The cenpB gene is not essential in mice (1998)
    Springer
    Chromosoma 107 (1998), S. 570-576 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract.  Centromere protein B (CENP-B) is a centromeric DNA-binding protein that binds to α-satellite DNA at the 17 bp CENP-B box sequence. The binding of CENP-B, along with other proteins, to α-satellite DNA sequences at the centromere, is thought to package the DNA into heterochromatin subjacent to the kinetochore of mitotic chromosomes. To determine the importance of CENP-B to kinetochore assembly and function, we generated a mouse null for the cenpB gene. The deletion removed part of the promoter and the entire coding sequence except for the carboxyl-terminal 35 amino acids of the CENP-B polypeptide. Mice heterozygous or homozygous for the cenpB null mutation are viable and healthy, with no apparent defect in growth and morphology. We have established mouse embryo fibroblasts from heterozygous and homozygous cenpB null littermates. Microscopic analysis, using immunofluorescence and electron microscopy of the cultured cells, indicated that the centromere-kinetochore complex was intact and identical to control cells. Mitosis was identical in fibroblasts derived from cenpB wild-type, heterozygous and null animals. Our studies demonstrate that CENP-B is not required for the assembly of heterochromatin or the kinetochore, or for completion of mitosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004120050343
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  • 2
    Electronic Resource
    Electronic Resource
    The molecular mechanisms of conidial germination (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 199 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The asexual spore, or conidium, is critical in the life cycle of many fungi because it is the primary means for dispersion and serves as a ‘safe house’ for the fungal genome in adverse environmental conditions. This review discusses the physiological process of germination, conidial adhesion and initiation of protein synthesis and also the regulatory pathways used to activate conidial germination. These include Ca2+/calmodulin-mediated signaling, the cyclic AMP/protein kinase A and the ras/mitogen-activated protein kinase pathways. Insights into the process of conidial germination will increase our understanding of the mechanisms of dormancy and sensing of environmental stimuli, and permit identification of novel therapeutic targets for the treatment of spore-borne fungal infections in plants and animals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10667.x
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  • 3
    Electronic Resource
    Electronic Resource
    Genetic and Functional Analysis of Beta Tubulin in Aspergillus nidulans (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 466 (1986), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1986.tb38380.x
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  • 4
    Electronic Resource
    Electronic Resource
    Production of Biologically Active Recombinant Human Lactoferrin in Aspergillus Oryzae (1992)
    [s.l.] : Nature Publishing Company
    Nature biotechnology 10 (1992), S. 784-789 
    Details
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] We report the production of recombinant human lactoferrin in Aspergillus oryzae. Expression of human lactoferrin (hLF), a 78 kD glycoprotein, was achieved by placing the cDNA under the control of the A. oryzae α–amylase promoter and the 3′ flanking region of the A. niger ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nbt0792-784
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  • 5
    Electronic Resource
    Electronic Resource
    Increasing tubC β-tubulin synthesis by placing it under the control of a benA β-Tubulin upstream sequence causes a reduction in benA β-tubulin level but has no effect on microtubule function (1990)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 16 (1990), S. 214-220 
    Details
    ISSN: 0886-1544
    Keywords: Aspergillus ; benomyl ; chimeric gene ; tubulin mutants ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We have constructed a chimeric β-tubulin gene that places the structural gene for the tubC β-tubulin of Axpergillus nidulans under the control of the benA β-tubulin promoter. Introduction of cither this chimeric gene or a second wild-type ben.A gene into a benomyl-resistant benA22 strain causes it to become benomyl sensitive, indicating that the introduced genes are functional. Analysis of the tubulin proteins synthesized in benA22 strains into which a second wild-type benA β-tubulin gene was transformed showed that the total amount of β-tubulin protein was the same as in the parental strain with a single benA gene. Thus the level of β-tubulin must be regulated. This was also true of transformants carrying an extra copy of the chimeric β-tubulin gene. The total amount of β-tubulin was the same as in the parental strain. Two-dimensional gel analysis showed that the endoge-nous benA22 and the introduced chimeric tubC gene contributed equally to the total β-tubulin pool. Th; fact that one-half of the benA β-tubulin could be replaced by tubC β-tubulin with no effect on the growth of the cells suggests that the benA and tubC β-tubulins are functionally interchangeable.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970160308
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  • 6
    Electronic Resource
    Electronic Resource
    Sequence, organization and expression of the core histone genes ofAspergillus nidulans (1990)
    Springer
    Molecular genetics and genomics 222 (1990), S. 416-424 
    Details
    ISSN: 1617-4623
    Keywords: Electrophoretic karyotype ; Coordinate gene expression ; Histone ; Aspergillus nidulans
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The core histone gene family ofAspergillus nidulans was characterized. The H2A, H2B and H3 genes are unique in theA. nidulans genome. In contrast there are two H4 genes, H4.1 and H4.2. As previously reported for the H2A gene (May and Morris 1987) introns also interrupt the other core histone genes. The H2B gene, like the H2A gene, is interrupted by three introns, the H3 and H4.1 gene are each interrupted by two introns and the H4.2 gene contains one intron. The position of the single intron in H4.2 is the same as that the first intron of the H4.1 gene. The H2A and H2B genes are arranged as a gene pair separated by approximately 600 by and are divergently transcribed. The H3 and H4.1 genes are similarly arranged and are separated by approximately 800 bp. The H4.2 gene is not closely linked to either the H2A-H2B or H3-H4.1 gene pairs. Using pulse field gel electrophoresis an electrophoretic karyotype was established forA. nidulans. This karyotype was used to assign the H3–H4.1 gene pair and the H4.2 gene to linkage group VIII and the H2A–H2B gene pair to either linkage group III or VI. The abundance of each of the histone messenger RNAs was determined to be cell cycle regulated but the abundance of the H4.2 mRNA appears to be regulated differently from the others.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00633848
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