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• W1796227644 abstract "NUC-1, a positive regulatory protein of Neurospora crassa, controls the expression of several unlinked target genes involved in phosphorus acquisition. The carboxy-terminal end of the NUC-1 protein has sequence similarity to the helix-loop-helix family of transcription factors. Bacterially expressed and in vitro-synthesized proteins, which consist of the carboxy-terminal portion of NUC-1, bind specifically to upstream sequences of two of its target genes, pho2+ and pho-4+. These upstream sequences contain the core sequence, CACGTG, a target for many helix-loop-helix proteins. A large loop region (47 amino acids) separates the helix I and helix II domains. Mutations and deletion within the loop region did not interfere with the in vitro or in vivo functions of the protein. Immediately carboxy-proximal to the helix II domain, the NUC-1 protein contains an atypical zipper domain which is essential for function. This domain consists of a heptad repeat of alanine and methionine rather than leucine residues. Analysis of mutant NUC-1 proteins suggests that the helix II and the zipper domains are essential for the protein dimerization, whereas the basic and the helix I domains are involved in DNA binding. The helix I domain, even though likely to participate in dimer formation while NUC-1 is bound to DNA, is not essential for in vitro dimerization." @default.
• W1796227644 created "2016-06-24" @default.
• W1796227644 creator A5027260604 @default.
• W1796227644 creator A5060991897 @default.
• W1796227644 date "1994-12-01" @default.
• W1796227644 modified "2023-09-27" @default.
• W1796227644 title "Analysis of the DNA-binding and dimerization activities of Neurospora crassa transcription factor NUC-1" @default.
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• W1796227644 doi "https://doi.org/10.1128/mcb.14.12.7816-7826.1994" @default.
• W1796227644 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/359321" @default.
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