Building Blocks for Plant Gene Assembly

Karimi, Mansour; Bleys, Annick; Vanderhaeghen, Rudy; Hilson, Pierre

doi:10.1104/pp.107.110411

Cited by 242 publications

(241 citation statements)

References 43 publications

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“…The vector pK7m34GW2-8m21GW3D was used for the simultaneous ectopic expression of MtCLE12 and MtCLE13 (Karimi et al, 2007). For promoter:GUS analysis, a 2-kb region upstream of MtCLE12 and MtCLE13 was isolated from genomic DNA based on the available genomic data (http://www.ncbi.nlm.nih.gov/).…”

Section: Biological Materialsmentioning

confidence: 99%

CLE Peptides Control Medicago truncatula Nodulation Locally and Systemically

Mortier

Herder²,

Whitford³

et al. 2010

Plant Physiology

297

409

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The CLAVATA3/embryo-surrounding region (CLE) peptides control the fine balance between proliferation and differentiation in plant development. We studied the role of CLE peptides during indeterminate nodule development and identified 25 MtCLE peptide genes in the Medicago truncatula genome, of which two genes, MtCLE12 and MtCLE13, had nodulation-related expression patterns that were linked to proliferation and differentiation. MtCLE13 expression was up-regulated early in nodule development. A high-to-low expression gradient radiated from the inner toward the outer cortical cell layers in a region defining the incipient nodule. At later stages, MtCLE12 and MtCLE13 were expressed in differentiating nodules and in the apical part of mature, elongated nodules. Functional analysis revealed a putative role for MtCLE12 and MtCLE13 in autoregulation of nodulation, a mechanism that controls the number of nodules and involves systemic signals mediated by a leucine-rich repeat receptor-like kinase, SUNN, which is active in the shoot. When MtCLE12 and MtCLE13 were ectopically expressed in transgenic roots, nodulation was abolished at the level of the nodulation factor signal transduction, and this inhibition involved long-distance signaling. In addition, composite plants with roots ectopically expressing MtCLE12 or MtCLE13 had elongated petioles. This systemic effect was not observed in transgenic roots ectopically expressing MtCLE12 and MtCLE13 in a sunn-1 mutant background, although nodulation was still strongly reduced. These results suggest multiple roles for CLE signaling in nodulation.

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Section: Biological Materialsmentioning

confidence: 99%

CLE Peptides Control Medicago truncatula Nodulation Locally and Systemically

Mortier

Herder²,

Whitford³

et al. 2010

Plant Physiology

297

409

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“…PCR products were purified and cloned into pENTR/D-TOPO (Thermo Fisher Scientific), sequenced, and then recombined with pEN-L4-2-R1 and pB7m24GW (Karimi et al, 2007) via a multiple gateway LR reaction (as described above). The final constructs were sequenced and named Prom35S: PPsPase1 and Prom35S:PECP1.…”

Section: Gene Overexpressing Linesmentioning

confidence: 99%

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

et al. 2018

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Phosphate starvation-mediated induction of the HAD-type phosphatases PPsPase1 (AT1G73010) and PECP1 (AT1G17710) has been reported in Arabidopsis (Arabidopsis thaliana). However, little is known about their in vivo function or impact on plant responses to nutrient deficiency. The preferences of PPsPase1 and PECP1 for different substrates have been studied in vitro but require confirmation in planta. Here, we examined the in vivo function of both enzymes using a reverse genetics approach. We demonstrated that PPsPase1 and PECP1 affect plant phosphocholine and phosphoethanolamine content, but not the pyrophosphate-related phenotypes. These observations suggest that the enzymes play a similar role in planta related to the recycling of polar heads from membrane lipids that is triggered during phosphate starvation. Altering the expression of the genes encoding these enzymes had no effect on lipid composition, possibly due to compensation by other lipid recycling pathways triggered during phosphate starvation. Furthermore, our results indicated that PPsPase1 and PECP1 do not influence phosphate homeostasis, since the inactivation of these genes had no effect on phosphate content or on the induction of molecular markers related to phosphate starvation. A combination of transcriptomics and imaging analyses revealed that PPsPase1 and PECP1 display a highly dynamic expression pattern that closely mirrors the phosphate status. This temporal dynamism, combined with the wide range of induction levels, broad expression, and lack of a direct effect on Pi content and regulation, makes PPsPase1 and PECP1 useful molecular markers of the phosphate starvation response.Plant growth is highly sensitive to a lack of phosphate (Pi); hence, the application of Pi fertilizers has become standard practice for high-throughput crop production (Cordell et al., 2009). Most phosphorus in the soil is not available to plants, as it is combined with other minerals or parts of organic compounds (Bieleski, 1973;Raghothama and Karthikeyan, 2005). Only a small fraction of soluble Pi (usually present at a concentration of ,10 mM in the soil) can be taken up by plants.Although growth is not optimal under limiting conditions, plants can withstand changing Pi concentrations within heterogeneous soils or in the external nutrient supply that can lead to reprogramming of their metabolism and architecture (Hammond et al., 2003;Péret et al., 2011;Plaxton and Tran, 2011). Root architecture can be modified to facilitate Pi uptake by favoring the development of lateral roots (at the expense of primary root elongation in many plants including Arabidopsis), increasing the density and length of root hairs, and limiting the development of aerial parts (López-Bucio et al., 2002;Svistoonoff et al., 2007;Gruber et al., 2013). Pi uptake mechanisms are enhanced at the root/soil interface, particularly through the stimulation of Pi transport activity (Mudge et al., 2002;Shin et al., 2004;Nussaume et al., 2011; Ayadi et al., 2015). In parallel, mobilization of Pi sources fr...

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“…The AtPRA1 promoter sequences were amplified from Arabidopsis genomic DNA by PCR (for primer sequences, see Supplemental Table S2) or obtained from the systematic analysis of the Arabidopsis promoterome database (Benhamed et al, 2008). Each PCR fragment was cloned into the pDONRP4P1R entry vector by BP reaction and subsequently transferred into the pMK7S*NFm14GW modular destination vector (Karimi et al, 2007) by attL 3 attR (LR) recombination reaction, resulting in a transcriptional fusion between the AtPRA1 promoters and the EGFP-GUS fusion. All constructs were transferred into the Agrobacterium tumefaciens C58C1Rif R strain harboring the pMP90 plasmid.…”

Section: Plant Growth Conditions and Plasmid Constructionmentioning

confidence: 99%

ThePRA1Gene Family in Arabidopsis

Kamei

Boruc²,

Vandepoele³

et al. 2008

Plant Physiology

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Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the vacuolar soluble N-ethylmaleimide-sensitive factor attachment receptor protein VAMP2. However, little is known about PRA1 family members in plants. Sequence analysis revealed that higher plants, compared with animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis (Arabidopsis thaliana) PRA1 (AtPRA1) proteins were found to homodimerize and heterodimerize in a manner corresponding to their phylogenetic distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly coexpressed with Rab GTPases and genes encoding vesicle transport proteins, suggesting an involvement in the vesicle trafficking process similar to that of their animal counterparts. Correspondingly, AtPRA1 proteins were localized in the endoplasmic reticulum, Golgi apparatus, and endosomes/ prevacuolar compartments, hinting at a function in both secretory and endocytic intracellular trafficking pathways. Taken together, our data reveal a high functional diversity of AtPRA1 proteins, probably dealing with the various demands of the complex trafficking system.

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Building Blocks for Plant Gene Assembly

Cited by 242 publications

References 43 publications

CLE Peptides Control Medicago truncatula Nodulation Locally and Systemically

CLE Peptides Control Medicago truncatula Nodulation Locally and Systemically

The Phosphate Fast-Responsive Genes PECP1 and PPsPase1 Affect Phosphocholine and Phosphoethanolamine Content

ThePRA1Gene Family in Arabidopsis

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