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  • Maltose fermentation  (2)
  • Capillary Zone Electrophoresis  (1)
  • Earth Resources and Remote Sensing  (1)
  • 1
    ISSN: 1432-0983
    Keywords: Key wordsMAL-activator ; Maltose fermentation ; Saccharomyces
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract MAL63 of the MAL6 locus and its homologues at the other MAL loci encode transcription activators required for the maltose-inducible expression of the MAL structural genes. We carried out a deletion analysis of LexA-MAL63 gene fusions to localize the functional domains of the Mal63 MAL-activator protein. Our results indicate that the sequence-specific DNA-binding domain of Mal63p is contained in residues 1–100; that residues 60–283 constitute a functional core region including the transactivation domain; that residues 251–299 are required to inhibit the activation function of Mal63p; and that the rest of the C-terminal region of the protein contains a maltose-responsive domain that acts to relieve the inhibitory effect on the activation function. Abundant overproduction of Mal63p does not overcome the negative regulation of MAL gene expression in the absence of maltose, suggesting that a titratable MAL-specific repressor similar to Gal80p is not involved in the negative regulation of the MAL-activator. A model for maltose-inducible autoregulation of the MAL-activator is presented.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0983
    Keywords: Key wordsMAL-activator ; Constitutive mutations ; Maltose fermentation ; Saccharomyces
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces MAL-activator regulates the maltose-inducible expression of the MAL structural genes encoding maltose permease and maltase. Constitutive MAL-activator mutant alleles of two types were identified. The first were truncation mutations deleting C-terminal residues 283–470 and the second contained a large number of alterations compared to inducible alleles scattered throughout the C-terminal 200 residues. We used site-directed in vitro mutagenesis of the inducible MAL63 and MAL63/23 genes to identify the residues responsible for the negative regulatory function of the C-terminal domain. Intragenic suppressors that restored the inducible phenotype to the constitutive mutants were identified at closely linked and more distant sites within the MAL-activator protein. MAL63/mal64 fusions of the truncated mutants suggest that residues in the N-terminal 100 residues containing the DNA-binding domain also modulate basal expression. Moreover, a transcription activator protein consisting of LexA(1–87)-Gal4(768–881)-Mal63(200–470) allowed constitutive reporter gene expression, suggesting that the C-terminal regulatory domain is not sufficient for maltose-inducible control of this heterologous activation domain. These results suggest that complex and very specific intramolecular protein–protein interactions regulate the MAL-activator.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1612-1112
    Keywords: Capillary Zone Electrophoresis ; Bacillus subtilis ; Tryptophanyl-tRNA synthetase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary The application of capillary zone electrophoresis to the study of interactions betweenBacillus subtilis tryptophanyl-tRNA synthetase (TrpRS) and tRNATrp is described. Significant changes in peak shape of tRNATrp incubated with TrpRS indicated the occurrence of interactions between TrpRS and tRNATrp in pH 8.0 Tris-HCl buffer containing 0.1 mmol L−1 EDTA and 1 mmol L−1−5 mmol L−1 mgCl2. Addition of Mg2+ decreased the electrophoretic mobility of tRNATrp, which illustrated that conformation of tRNATrp depended on Mg2+. The dissociation constant of the TrpRS-tRNATrp complex was estimated to be 0.63 μmol L−1 at 25°C in buffer solution.
    Type of Medium: Electronic Resource
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  • 4
    Publication Date: 2019-07-20
    Description: The AQUA, SNPP, and NOAA 18-20 PM sun-synchronous satellites were designed with similar local time, local solarzenith angles, and overlapping temporal coverage. Although the satellites are expected to have fixed local equator-crossing time, during the satellite lifetime, the equator-crossing times of these satellites drift. For NOAA 18-19, the driftin equator-crossing time is significant (few hours) and no correction has been done over the lifetime. For SNPP andAQUA, correction in the orbital inclination angle was periodically performed to maintain the equator-crossing timearound the designed value. The impact of systematic drift of the local observation time during the satellite life cycle canbe significant and should be accounted for when using multi-year time series of satellite products in long-termenvironmental studies. In this paper, the equator-crossing time drift of AQUA, SNPP, and NOAA 18-20, the correctionof SNPP and AQUA equator-crossing time via orbital inclination angle change, and the consequent local solar zenithangle variation are evaluated. The impact of such drift on low-latitude mean brightness temperature trend derived fromthe similar ~11 m thermal emissive channel of AQUA MODIS CH31, SNPP Visible Infrared Imaging RadiometerSuite (VIIRS) CH15 and NOAA 18-19 HIRS CH08 are analyzed. The drift in the mean brightness temperature measuredby these sensors is combined as a function of local time and analyzed using diurnal cycle analysis. The mean brightnesstemperature drift for SNPP VIIRS is reconciled within the context of much larger temperature drift of NOAA 18-19.
    Keywords: Earth Resources and Remote Sensing
    Type: GSFC-E-DAA-TN66863 , Earth Observing Systems XXIII; 10764; 107641U|SPIE Optics + Photonics; Aug 19, 2018 - Aug 23, 2018; San Diego, CA; United States
    Format: application/pdf
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