| Literature DB >> 31010807 |
Angad Garg1, Yehuda Goldgur2, Ana M Sanchez3, Beate Schwer3, Stewart Shuman4.
Abstract
Pho7 is the Schizosaccharomyces pombe fission yeast Zn2Cys6 transcriptional factor that drives a response to phosphate starvation in which phosphate acquisition genes are upregulated. Here we report a crystal structure at 1.6-Å resolution of the Pho7 DNA-binding domain (DBD) bound at its target site 2 in the pho1 promoter (5'-TCGGAAATTAAAAA). Comparison to the previously reported structure of Pho7 DBD in complex with its binding site in the tgp1 promoter (5'-TCGGACATTCAAAT) reveals shared determinants of target site specificity as well as variations in the protein-DNA interface that accommodate different promoter DNA sequences. Mutagenesis of Pho7 amino acids at the DNA interface identified nucleobase contacts at the periphery of the footprint that are essential for the induction of pho1 expression in response to phosphate starvation and for Pho7 binding to site 1 in the pho1 promoter.Entities:
Keywords: DNA-protein interaction; Schizosaccharomyces pombezzm321990; mutagenesis; protein structure; transcription factor
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Year: 2019 PMID: 31010807 PMCID: PMC6580706 DOI: 10.1128/MCB.00132-19
Source DB: PubMed Journal: Mol Cell Biol ISSN: 0270-7306 Impact factor: 4.272