ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Isolation and characterization of nickel-accumulating yeasts (1997)
    Springer
    Applied microbiology and biotechnology 48 (1997), S. 373-378 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract We selected three yeast strains that efficiently remove heavy metal ions from aqueous solution. We first screened yeasts that grew in the presence of 2 mM NiCl2 among our stock of wild yeasts, and then selected those that removed Ni most efficiently from aqueous solution. These strains also removed Cu and Zn from aqueous solution and were identified as Candida species. Ni uptake was efficient at pH between 4.0 and 7.0, but less efficient at pH below 3.0. The amount of Ni taken up by the yeast cells was proportional to the initial concentration of NiCl2 below about 4 mM Ni. The cells retained the abilities to remove Ni after treatment with 10 mM EDTA or 1 M HCl for repeated usage, or after heat treatment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051065
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Molecular cloning and characterization of a gene encoding glutaminase from Aspergillus oryzae (2000)
    Springer
    Applied microbiology and biotechnology 54 (2000), S. 59-68 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  A glutaminase from Aspergillus oryzae was purified and its molecular weight was determined to be 82,091 by matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Purified glutaminase catalysed the hydrolysis not only of l-glutamine but also of d-glutamine. Both the molecular weight and the substrate specificity of this glutaminase were different from those reported previously [Yano et al. (1998) J Ferment Technol 66: 137–143]. On the basis of its internal amino acid sequences, we have isolated and characterized the glutaminase gene (gtaA) from A. oryzae. The gtaA gene had an open reading frame coding for 690 amino acid residues, including a signal peptide of 20 amino acid residues and a mature protein of 670 amino acid residues. In the 5′-flanking region of the gene, there were three putative CreAp binding sequences and one putative AreAp binding sequence. The gtaA structural gene was introduced into A. oryzae NS4 and a marked increase in activity was detected in comparison with the control strain. The gtaA gene was also isolated from Aspergillus nidulans on the basis of the determined nucleotide sequence of the gtaA gene from A. oryzae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530000329
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Cloning, characterization and overproduction of nuclease S1 gene (nucS) from Aspergillus oryzae (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 425-431 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  The nuclease S1 gene (nucS) from Aspergillus oryzae was isolated using a polymerase-chain-reaction-amplified DNA fragment as a probe, and a 2.6-kb SalI-EcoRI fragment containing the nucS gene was sequenced. It was deduced that the nucS gene had two short introns, 49 and 50 nucleotides in length. The nucS gene had an open-reading frame of 963 base pairs and coded for a protein of 287 amino acid residues, comprising the signal peptide of 20 amino acids and a mature protein of 267amino acids. The deduced amino acid sequence agreed well with the published amino acid sequence except for one substitution. Southern hybridization analysis showed that the nucS gene existed as a single copy in the A. oryzae chromosome. When the structural gene of nucS was fused with the promoter of the glaA gene and introduced into A. oryzae, the yield of secreted nuclease S1 increased about 100-fold compared with the recipient strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050577
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Cloning, characterization and overproduction of nuclease S1 gene (nucS) from Aspergillus oryzae (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 425-431 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The nuclease S1 gene (nucS) from Aspergillus oryzae was isolated using a polymerase-chain-reaction-amplified DNA fragment as a probe, and a 2.6-kb SalI-EcoRI fragment containing the nucS gene was sequenced. It was deduced that the nucS gene had two short introns, 49 and 50 nucleotides in lenght. The nucS gene had an open-reading frame of 963 base pairs and coded for a protein of 287 amino acid residues, comprising the signal peptide of 20 amino acids and a mature protein of 267 amino acids. The deduced amino acid sequence agreed well with the published amino acid sequence except for one substitution. Southern hybridization analysis showed that the nucS gene existed as a single copy in the A. oryzae chromosome. When the structural gene of nucS was fused with the promoter of the glaA gene and introduced into A. oryzae, the yield od secreted nuclease S1 increased about 100-fold compared with the recipient strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169939
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Improvement of promoter activity by the introduction of multiple copies of the conserved region III sequence, involved in the efficient expression of Aspergillus oryzae amylase-encoding genes (1998)
    Springer
    Applied microbiology and biotechnology 50 (1998), S. 459-467 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The role of the conserved sequence region III in the promoter regions of the amylase-encoding genes amyB, glaA and agdA of Aspergillus oryzae was examined. Introduction of multiple copies of the region III fragment into the agdA promoter resulted in a significant increase in promoter activity at the transcriptional level. This result suggests that the fragment comprising region III consists of one or more cis-acting sequence(s). Moreover, expression of the agdA gene under the control of the improved agdA promoter resulted in efficient overproduction of α -glucosidase, even in the presence of glucose. Thus, overexpression of genes controlled by the improved promoter incorporating region III is possible. Interestingly, expression of the amyB and glaA genes in the transformant was strongly repressed. This result suggests that the trans-acting regulatory protein(s) that interact with region III are common to these amylase genes and that the titration of regulatory protein(s) reduced the expression of the amyB and glaA genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051321
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Purification and characterization of isoamyl acetate-hydrolyzing esterase encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant Escherichia coli (2000)
    Springer
    Applied microbiology and biotechnology 53 (2000), S. 596-600 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The IAH1 gene of Saccharomyces cerevisiae encodes an esterase that preferentially acts on isoamyl acetate; however, the enzyme has not yet been completely purified from the yeast S. cerevisiae. We constructed the IAH1 gene expression system in Escherichia coli, and purified the IAH1 gene product (Iah1p). The amount of Iah1p produced by recombinant E. coli was more than 40% of total cellular proteins. The molecular size of Iah1p was 28 kDa by SDS-polyacrylamide gel electrophoresis. Judging from the molecular weight estimation by gel filtration of purified Iah1p, the enzyme was thought to be a homodimer. The K m values for isoamyl acetate and isobutyl acetate were 40.3 mM and 15.3 mM, respectively. The enzyme activity was inhibited by Hg2+, p-chloromercuribenzoate, and diisopropylfluorophosphate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051662
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Deletion analysis of promoter elements of the Aspergillus oryzae agdA gene encoding α-glucosidase (1996)
    Springer
    Current genetics 30 (1996), S. 432-438 
    Details
    ISSN: 1432-0983
    Keywords: Key words Aspergillus oryzae ; α-Glucosidase ; Deletion analysis ; Functional element
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The nucleotide sequence of a 1.5-kb fragment of the promoter region of the Aspergillus oryzae agdA gene encoding α-glucosidase was determined. A comparison with the promoter regions of other Aspergillus amylase genes indicated that there are three highly conserved sequences, designated Regions I, II and III, located at −670 nt, −596 nt and −544 nt relative to the start codon, respectively. The function of these consensus sequences in the agdA promoter was investigated by deletion analysis of a promoter fusion with the Escherichia coli uidA gene, using the niaD homologous-transformation system. Deletion of the upstream half of Region III (IIIa; −544 to −529) resulted in a more than 90% reduction in GUS activity and abolished maltose induction, suggesting that Region IIIa is a functionally essential element for high-level expression and maltose induction. Deletion of Region I and the downstream half of Region III (IIIb; −521 to −511) resulted in a significant reduction in GUS activity, but did not affect maltose induction. This suggested that these two elements most likely contain sequences involved in efficient expression in cooperation with Region IIIa. In addition, deletion of a 340-bp region between Region IIIb and the putative TATA box resulted in a 2-fold increase in activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050153
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 8
    Electronic Resource
    Electronic Resource
    Cloning and characterization of a gene (arpA) from Aspergillus oryzae encoding an actin-related protein required for normal nuclear distribution and morphology of conidiophores (1999)
    Springer
    Molecular genetics and genomics 262 (1999), S. 758-767 
    Details
    ISSN: 1617-4623
    Keywords: Key words Actin-related protein ; Dynactin ; Nuclear migration ; Aspergillus oryzae ; Hyper-branching hyphae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have isolated the arpA gene from Aspergillus oryzae as a homologue of the Neurospora crassa ro-4 gene. In N. crassa, mutations in the ro-4 gene, which encodes a major component of the dynactin complex Arp1, causes curling of hyphae and abnormalities in nuclear distribution. The arpA gene contains two introns and encodes a polypeptide of 381 amino acids, with a 78% sequence identity to the N. crassa Arp1. Overexpression of the arpA gene causes a defect in nuclear migration into elongating hyphae of germlings in A. oryzae. We constructed arpA disruptant strains of A. oryzae. The arpA null mutants showed poor growth and hyper-branched mycelia, as well as a nuclear distribution defect. Scanning electron microscopy revealed that the arpA null mutant has an aberrant conidiophore morphology with irregular phialides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380051138
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 9
    Electronic Resource
    Electronic Resource
    The protease activity of a calpain-like cysteine protease in Saccharomyces cerevisiae is required for alkaline adaptation and sporulation (1999)
    Springer
    Molecular genetics and genomics 260 (1999), S. 559-568 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsSaccharomyces cerevisiae ; Calpain ; Alkaline adaptation ; Sporulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Saccharomyces cerevisiae has only one putative gene (designated CPL1) for a cysteine protease with a protease domain similar to that of calpain. This gene product shows significant sequence similarity to PalBp, a fungal (Emericella nidulans) calpain-like protease that is responsible for adaptation under alkaline conditions, both in the protease domain and the domain following the protease domain. CPL1 disruptant strains show impaired growth at alkaline pH, but no obvious growth defects under acidic pH conditions. This phenotype is complemented by the wild-type CPL1 gene, and its protease activity is essential for complementation. Disruption of CPL1 also causes reduced sporulation efficiency and promotes the degradation of the transcription factor Rim101p, which is involved in the sporulation pathway and has been shown to accumulate in a C-terminally truncated, active form under alkaline conditions. Furthermore, expression of the C-terminally truncated Rim101p suppressed the alkaline sensitivity associated with CPL1 disruption. These results indicate that a calpain-like cysteine protease, Cpl1p, plays an important role in alkaline adaptation and sporulation processes, via regulation of the turnover and processing of the transcription factor Rim101p.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050929
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 10
    facet.materialart.
    Unknown
    Upper limit on the flux of photons with energies above1019  eVusing the Telescope Array surface detector (2013)
    American Physical Society
    Details
    Publication Date: 2013-12-03
    Print ISSN: 1550-7998
    Electronic ISSN: 1550-2368
    Topics: Physics
    Published by American Physical Society
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...