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1.
Plant Physiol ; 175(3): 1105-1120, 2017 Nov.
Article in English | MEDLINE | ID: mdl-28874520

ABSTRACT

In Solanaceae, the S-specific interaction between the pistil S-RNase and the pollen S-Locus F-box protein controls self-incompatibility (SI). Although this interaction defines the specificity of the pollen rejection response, the identification of three pistil essential modifier genes unlinked to the S-locus (HT-B, 120K, and NaStEP) unveils a higher degree of complexity in the pollen rejection pathway. We showed previously that NaStEP, a stigma protein with homology with Kunitz-type protease inhibitors, is essential to SI in Nicotiana spp. During pollination, NaStEP is taken up by pollen tubes, where potential interactions with pollen tube proteins might underlie its function. Here, we identified NaSIPP, a mitochondrial protein with phosphate transporter activity, as a novel NaStEP-interacting protein. Coexpression of NaStEP and NaSIPP in pollen tubes showed interaction in the mitochondria, although when expressed alone, NaStEP remains mostly cytosolic, implicating NaSIPP-mediated translocation of NaStEP into the organelle. The NaSIPP transcript is detected specifically in mature pollen of Nicotiana spp.; however, in self-compatible plants, this gene has accumulated mutations, so its coding region is unlikely to produce a functional protein. RNA interference suppression of NaSIPP in Nicotiana spp. pollen grains disrupts the SI by preventing pollen tube inhibition. Taken together, our results are consistent with a model whereby the NaStEP and NaSIPP interaction, in incompatible pollen tubes, might destabilize the mitochondria and contribute to arrest pollen tube growth.


Subject(s)
Mitochondrial Proteins/metabolism , Nicotiana/metabolism , Phosphate Transport Proteins/metabolism , Plant Proteins/metabolism , Self-Incompatibility in Flowering Plants , Gene Expression Regulation, Plant , Mitochondria/metabolism , Mitochondrial Proteins/chemistry , Models, Molecular , Mutation/genetics , Phosphate Transport Proteins/chemistry , Plant Cells/metabolism , Plant Proteins/chemistry , Pollen Tube/metabolism , Protein Binding , Protein Transport , RNA, Messenger/genetics , RNA, Messenger/metabolism , Saccharomyces cerevisiae/metabolism , Subcellular Fractions/metabolism , Nicotiana/genetics
2.
J Exp Bot ; 58(10): 2573-82, 2007.
Article in English | MEDLINE | ID: mdl-17562688

ABSTRACT

Phosphorus deficiency is one of the major nutrient stresses affecting plant growth. Plants respond to phosphate (Pi) deficiency through multiple strategies, including the synthesis of high-affinity Pi transporters. In this study, the expression pattern of one putative wheat high-affinity phosphate transporter, TaPT2, was examined in roots and leaves under Pi-deficient conditions. TaPT2 transcript levels increased in roots of Pi-starved plants. A 579 bp fragment of the TaPT2 promoter is sufficient to drive the expression of the GUS reporter gene specifically in roots of Pi-deprived wheat. This TaPT2 promoter fragment was also able to drive expression of the GUS reporter gene in transgenic Arabidopsis thaliana, under similar growth conditions. Conserved regions and candidate regulatory motifs were detected by comparing this promoter with Pi transporter promoters from barley, rice, and Arabidopsis. Altogether, these results indicate that there are conserved cis-acting elements and trans-acting factors that enable the TaPT2 promoter to be regulated in a tissue-specific and Pi-dependent fashion in both monocots and dicots.


Subject(s)
Phosphate Transport Proteins/genetics , Plant Proteins/genetics , Promoter Regions, Genetic , Triticum/genetics , Arabidopsis/genetics , Base Sequence , Computational Biology , Conserved Sequence , Gene Expression Regulation, Plant , Glucuronidase/analysis , Molecular Sequence Data , Phosphate Transport Proteins/chemistry , Phosphates/metabolism , Plant Proteins/chemistry , Plant Roots/genetics , Plant Roots/metabolism , Plants, Genetically Modified/metabolism , Sequence Alignment , Sequence Analysis, DNA , Sequence Analysis, Protein
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