PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 Is a Plant-Specific SEC12-Related Protein That Enables the Endoplasmic Reticulum Exit of a High-Affinity Phosphate Transporter in Arabidopsis [W]
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چکیده
منابع مشابه
PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 is a plant-specific SEC12-related protein that enables the endoplasmic reticulum exit of a high-affinity phosphate transporter in Arabidopsis.
PHOSPHATE TRANSPORTER1 (PHT1) genes encode phosphate (Pi) transporters that play a fundamental role in Pi acquisition and remobilization in plants. Mutation of the Arabidopsis thaliana PHOSPHATE TRANSPORTER TRAFFIC FACILITATOR1 (PHF1) impairs Pi transport, resulting in the constitutive expression of many Pi starvation-induced genes, increased arsenate resistance, and reduced Pi accumulation. PH...
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An Arabidopsis genomic sequence was recently shown to share similarity with bacterial and eukaryotic phosphate (Pi) transporters. We have cloned the corresponding cDNA, which we named Pht2;1, and subsequently performed gene expression studies and functional analysis of the protein product. The cDNA encodes a 61-kD protein with a putative topology of 12 transmembrane (TM) domains interrupted by ...
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Using a high-affinity phosphate transporter gene of Arabidopsis thaliana, PHT1, as a probe, three Arabidopsis homologs were isolated, named PHT4, PHT5 and PHT6, in addition to the previously isolated PHT2 and PHT3. The amino acid sequences deduced from the three nucleotides were 32-42% homologous with microbial phosphate transporters of Saccharomyces cerevisiae (PHO84), Neurospora crassa (PHO-5...
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The uptake and distribution of Pi in plants requires multiple Pi transport systems that must function in concert to maintain homeostasis throughout growth and development. The Pi transporter PHT2;1 of Arabidopsis shares similarity with members of the Pi transporter family, which includes Na(+)/Pi symporters of fungal and animal origin and H(+)/Pi symporters of bacterial origin. Sequence compari...
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ژورنال
عنوان ژورنال: The Plant Cell
سال: 2005
ISSN: 1532-298X
DOI: 10.1105/tpc.105.036640