ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
  • 1
    Digitale Medien
    Digitale Medien
    Functional domain analysis of the Saccharomyces MAL-activator (1999)
    Springer
    Current genetics 36 (1999), S. 1-12 
    Details
    ISSN: 1432-0983
    Schlagwort(e): Key wordsMAL-activator ; Maltose fermentation ; Saccharomyces
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s002940050466
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Artikel (Nationallizenzen)
    Volltext
  • 2
    Digitale Medien
    Digitale Medien
    Alterations in the Saccharomyces MAL-activator cause constitutivity but can be suppressed by intragenic mutations (2000)
    Springer
    Current genetics 38 (2000), S. 233-240 
    Details
    ISSN: 1432-0983
    Schlagwort(e): Key wordsMAL-activator ; Constitutive mutations ; Maltose fermentation ; Saccharomyces
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s002940000161
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Artikel (Nationallizenzen)
    Volltext
  • 3
    Digitale Medien
    Digitale Medien
    Application of capillary zone electrophoresis to the study of interactions betweenBacillus subtilis tryptophanyl-tRNA synthetase and tRNATrp (1998)
    Springer
    Chromatographia 48 (1998), S. 268-272 
    Details
    ISSN: 1612-1112
    Schlagwort(e): Capillary Zone Electrophoresis ; Bacillus subtilis ; Tryptophanyl-tRNA synthetase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: 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.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02467682
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
    Artikel (Nationallizenzen)
    Volltext
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...