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1.
Physiol Plant ; 171(4): 802-808, 2021 Apr.
Article in English | MEDLINE | ID: mdl-33280129

ABSTRACT

Urea is the most used nitrogenous fertilizer worldwide and an important nitrogen-containing plant metabolite. Despite its major use as fertilizer, its direct uptake is limited due to the ubiquitous presence of bacterial urease, which leads to the formation of ammonium. In this review, we will focus mainly on the more recent research about the high-affinity urea transporter function in nitrogen-deficient conditions. The effective use of nitrogenous compounds is essential for plants to be able to deal with nitrogen-deficient conditions. Leaf senescence, either induced by development and/or by nitrogen deficiency, plays an important role in the efficient use of already assimilated nitrogen. Proteinaceous nitrogen is set free through catabolic reactions: the released amino acids from protein catabilization are in turn catabolized leading to an accumulation of ammonium and urea. The concentration and conversion to transportable forms of nitrogen, e.g. amino acids like glutamine and asparagine, are coordinated around the vascular tissue. Urea itself can be translocated directly over the phloem by a mechanism that involves DUR3, or it is converted by urease to ammonium and assimilated again into amino acids. The details of the high-affinity transporter function in this physiological context and the implications for crop yield are explained.


Subject(s)
Arabidopsis , Biological Transport , Fertilizers , Nitrogen , Urea
2.
Physiol Plant ; 171(4): 703-713, 2021 Apr.
Article in English | MEDLINE | ID: mdl-33090485

ABSTRACT

BOR1 is an efflux transporter of boron (B), responsible for loading B into the xylem. It has been reported that nitrate (NO3 - ) concentrations significantly influence B concentrations in leaves and BOR1 mRNA accumulation in roots. Here, to unravel the interactive effects of B and NO3 - on plant growth and the function of BOR1 under the combination of B and NO3 - , seedling growth was analyzed in Col-0 and bor1 mutants. The growth of bor1 mutants was negatively affected by high NO3 - but neither by potassium chloride (KCl) nor ammonium (NH4 + ) under low B conditions, suggesting the involvement of BOR1 in growth under high NO3 - . Mutants of bor2 and bor4 did not exhibit such growth responses, suggesting that this effect was specific to BOR1 among the BORs tested. Under low B conditions, loss of the BOR1 function led to a more significant decrease in B concentrations in the presence of high NO3 - compared to normal NO3 - . Additionally, grafting experiments demonstrated that these effects of NO3 - occurred when BOR1 is absent in roots. High NO3 - treatment elevated BOR1 mRNA accumulation while the BOR1 protein accumulation was downregulated. These apparent opposite responses indicated that the transcriptional and (post-)translational regulations follow different patterns. Our work provides evidence of a novel regulation of BOR1 and another B transport system by both B and NO3 - in an interactive manner.


Subject(s)
Arabidopsis Proteins , Arabidopsis , Antiporters , Arabidopsis/genetics , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Boron , Nitrates , Plant Roots/genetics , Plant Roots/metabolism
3.
Physiol Plant ; 167(1): 75-89, 2019 Sep.
Article in English | MEDLINE | ID: mdl-30426495

ABSTRACT

Nitrogen is one of the most important elements for plant growth, and urea is one of the most frequently used nitrogen fertilizers worldwide. Besides the exogenously-supplied urea to the soil, urea is endogenously synthesized during secondary nitrogen metabolism. Here, we investigated the contribution of a urea transporter, DUR3, to rice production using a reverse genetic approach combined with localization studies. Tos17 insertion lines for DUR3 showed a 50% yield reduction in hydroponic culture, and a 26.2% yield reduction in a paddy field, because of decreased grain filling. Because shoot biomass production and shoot total N was not reduced, insertion lines were disordered not only in nitrogen acquisition but also in nitrogen allocation. During seed development, DUR3 insertion lines accumulated nitrogen in leaves and could not sufficiently develop their panicles, although shoot and root dry weights were not significantly different from the wild-type. The urea concentration in old leaf harvested from DUR3 insertion lines was lower than that in wild-type. DUR3 promoter-dependent ß-glucuronidase (GUS) activity was localized in vascular tissue and the midribs of old leaves. These results indicate that DUR3 contributes to nitrogen translocation and rice yield under nitrogen-deficient and field conditions.


Subject(s)
Membrane Transport Proteins/metabolism , Nitrogen/metabolism , Oryza/metabolism , Plant Leaves/metabolism , Plant Proteins/metabolism , Plant Shoots/metabolism , Urea Transporters
4.
Plant J ; 93(6): 992-1006, 2018 03.
Article in English | MEDLINE | ID: mdl-29356222

ABSTRACT

Ammonium influx into plant roots via the high-affinity transport system (HATS) is down-modulated under elevated external ammonium, preventing ammonium toxicity. In ammonium-fed Arabidopsis, ammonium transporter 1 (AMT1) trimers responsible for HATS activity are allosterically inactivated in a dose-dependent manner via phosphorylation of the conserved threonine at the carboxyl-tail by the calcineurin B-like protein 1-calcineurin B-like protein-interacting protein kinase 23 complex and other yet unidentified protein kinases. Using transcriptome and reverse genetics in ammonium-preferring rice, we revealed the role of the serine/threonine/tyrosine protein kinase gene OsACTPK1 in down-modulation of HATS under sufficient ammonium. In wild-type roots, ACTPK1 mRNA and protein accumulated dose-dependently under sufficient ammonium. To determine the function of ACTPK1, two independent mutants lacking ACTPK1 were produced by retrotransposon Tos17 insertion. Compared with segregants lacking insertions, the two mutants showed decreased root growth and increased shoot growth under 1 mm ammonium due to enhanced ammonium acquisition, via aberrantly high HATS activity, and use. Furthermore, introduction of OsACTPK1 cDNA fused to the synthetic green fluorescence protein under its own promoter complemented growth and the HATS influx, and suggested plasma membrane localization. Root cellular expression of OsACTPK1 also overlapped with that of ammonium-induced OsAMT1;1 and OsAMT1;2. Meanwhile, threonine-phosphorylated AMT1 levels were substantially decreased in roots of ACTPK1-deficient mutants grown under sufficient ammonium. Bimolecular fluorescence complementation assay further confirmed interaction between ACTPK1 and AMT1;2 at the cell plasma membrane. Overall, these findings suggest that ACTPK1 directly phosphorylates and inactivates AMT1;2 in rice seedling roots under sufficient ammonium.


Subject(s)
Ammonium Compounds/metabolism , Gene Expression Profiling , Oryza/genetics , Plant Proteins/genetics , Protein Serine-Threonine Kinases/genetics , Seedlings/genetics , Biological Transport/genetics , Cation Transport Proteins/genetics , Cation Transport Proteins/metabolism , Gene Expression Regulation, Developmental , Gene Expression Regulation, Plant , Mutation , Oryza/growth & development , Oryza/metabolism , Phosphorylation , Plant Proteins/metabolism , Plant Roots/genetics , Plant Roots/growth & development , Plant Roots/metabolism , Protein Binding , Protein Serine-Threonine Kinases/metabolism , Seedlings/growth & development , Seedlings/metabolism
5.
Front Plant Sci ; 6: 74, 2015.
Article in English | MEDLINE | ID: mdl-25741355

ABSTRACT

In higher plants cysteine biosynthesis is catalyzed by O-acetylserine(thiol)lyase (OASTL) and represents the last step of the assimilatory sulfate reduction pathway. It is mainly regulated by provision of O-acetylserine (OAS), the nitrogen/carbon containing backbone for fixation of reduced sulfur. OAS is synthesized by Serine acetyltransferase (SERAT), which reversibly interacts with OASTL in the cysteine synthase complex (CSC). In this study we identify and characterize the SERAT gene family of the crop plant Vitis vinifera. The identified four members of the VvSERAT protein family are assigned to three distinct groups upon their sequence similarities to Arabidopsis SERATs. Expression of fluorescently labeled VvSERAT proteins uncover that the sub-cellular localization of VvSERAT1;1 and VvSERAT3;1 is the cytosol and that VvSERAT2;1 and VvSERAT2;2 localize in addition in plastids and mitochondria, respectively. The purified VvSERATs of group 1 and 2 have higher enzymatic activity than VvSERAT3;1, which display a characteristic C-terminal extension also present in AtSERAT3;1. VvSERAT1;1 and VvSERAT2;2 are evidenced to form the CSC. CSC formation activates VvSERAT2;2, by releasing CSC-associated VvSERAT2;2 from cysteine inhibition. Thus, subcellular distribution of SERAT isoforms and CSC formation in cytosol and mitochondria is conserved between Arabidopsis and grapevine. Surprisingly, VvSERAT2;1 lack the canonical C-terminal tail of plant SERATs, does not form the CSC and is almost insensitive to cysteine inhibition (IC50 = 1.9 mM cysteine). Upon sulfate depletion VvSERAT2;1 is strongly induced at the transcriptional level, while transcription of other VvSERATs is almost unaffected in sulfate deprived grapevine cell suspension cultures. Application of abiotic stresses to soil grown grapevine plants revealed isoform-specific induction of VvSERAT2;1 in leaves upon drought, whereas high light- or temperature- stress hardly trigger VvSERAT2;1 transcription.

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