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  • Nitrogen regulation  (1)
  • UAS  (1)
  • 1
    ISSN: 1617-4623
    Keywords: Neurospora ; Nitrogen regulation ; NIT2 DNA binding ; GATA proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract NIT2, a positive-acting regulatory protein in Neurospora crassa, activates the expression of a series of unlinked structural genes that encode nitrogen catabolic enzymes. NIT2 binding sites in the promoter regions of nit3, alc and lao have at least two GATA sequence elements. We have examined the binding affinity of the NIT2 protein for the yeast DAL5 wild-type upstream activation sequence UASNTR, which contains two GATA elements, and for a series of mutated binding sites, each differing from the wild-type site by a single base. Substitution for individual nucleotides within 5′ or 3′ sequences that flank the GATA elements had only modest effects upon NIT2 binding. In contrast, nearly all substitutions within the GATA elements almost completely eliminated NIT2 binding, demonstrating the importance of the GATA sequence for NIT2 binding. Four high-affinity binding sites for the NIT2 protein were found within a central region of the nit-2 gene itself.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; UAS ; promoter ; transcription ; nitrogen metabolism ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: UASNTR, the UAS responsible for nitrogen catabolite repression-sensitive transcriptional activation of many nitrogen catabolic genes in Saccharomyces cerevisiae, has been previously thought to operate only as a pair of closely related dodecanucleotide sites each containing the sequence GATAA at its core. Here we show that a single UASNTR site is also able to combine with another unrelated cis-acting element to mediate transcription as well. In one instance the unrelated cis-acting element was TTTGTTTAC situated upstream of GLN1, while in another the cis-acting element was the one previously shown to bind the PUT3 protein. When a UASNTR site functions in combination with an unrelated site, the regulatory responses observed are a hybrid consisting of characteristics derived from both the UASNTR site and the unrelated site as well. These observations resolve several significant inconsistencies that have plagued studies focused on elucidation of the mechanisms involved in the global regulation of nitrogen catabolism.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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