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      A conserved MYB transcription factor involved in phosphate starvation signaling both in vascular plants and in unicellular algae.

      Genes & development
      Alleles, Amino Acid Sequence, Animals, Apoenzymes, chemistry, classification, genetics, metabolism, Arabidopsis, Arabidopsis Proteins, physiology, Base Sequence, Cell Nucleus, Chlamydomonas reinhardtii, Conserved Sequence, DNA, Plant, analysis, DNA-Binding Proteins, Deoxyribodipyrimidine Photo-Lyase, Fungal Proteins, Green Fluorescent Proteins, Luminescent Proteins, Membrane Glycoproteins, Molecular Sequence Data, Mutation, Phosphates, Phylogeny, Plant Proteins, Protein Structure, Tertiary, Proto-Oncogene Proteins c-myb, Sequence Homology, Amino Acid, Signal Transduction, Transcription Factors, Transcription, Genetic

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          Abstract

          Plants have evolved a number of adaptive responses to cope with growth in conditions of limited phosphate (Pi) supply involving biochemical, metabolic, and developmental changes. We prepared an EMS-mutagenized M(2) population of an Arabidopsis thaliana transgenic line harboring a reporter gene specifically responsive to Pi starvation (AtIPS1::GUS), and screened for mutants altered in Pi starvation regulation. One of the mutants, phr1 (phosphate starvation response 1), displayed reduced response of AtIPS1::GUS to Pi starvation, and also had a broad range of Pi starvation responses impaired, including the responsiveness of various other Pi starvation-induced genes and metabolic responses, such as the increase in anthocyanin accumulation. PHR1 was positionally cloned and shown be related to the PHOSPHORUS STARVATION RESPONSE 1 (PSR1) gene from Chlamydomonas reinhardtii. A GFP::PHR1 protein fusion was localized in the nucleus independently of Pi status, as is the case for PSR1. PHR1 is expressed in Pi sufficient conditions and, in contrast to PSR1, is only weakly responsive to Pi starvation. PHR1, PSR1, and other members of the protein family share a MYB domain and a predicted coiled-coil (CC) domain, defining a subtype within the MYB superfamily, the MYB-CC family. Therefore, PHR1 was found to bind as a dimer to an imperfect palindromic sequence. PHR1-binding sequences are present in the promoter of Pi starvation-responsive structural genes, indicating that this protein acts downstream in the Pi starvation signaling pathway.

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