scholarly journals Selenate-resistant mutants of Arabidopsis thaliana identify Sultr1;2, a sulfate transporter required for efficient transport of sulfate into roots

2002 ◽  
Vol 29 (4) ◽  
pp. 475-486 ◽  
Author(s):  
Nakako Shibagaki ◽  
Alan Rose ◽  
Jeffrey P. McDermott ◽  
Toru Fujiwara ◽  
Hiroaki Hayashi ◽  
...  
1987 ◽  
Vol 206 (2) ◽  
pp. 200-206 ◽  
Author(s):  
Mark A. Estelle ◽  
Chris Somerville

2005 ◽  
Vol 52 (3) ◽  
pp. 374-380 ◽  
Author(s):  
L. A. Volkova ◽  
A. B. Burgutin ◽  
O. P. Soldatova ◽  
T. A. Ezhova ◽  
P. V. Lapshin

2001 ◽  
pp. 38-39
Author(s):  
M. Awazuhara ◽  
H. Takahashi ◽  
A. Watanabe-Takahashi ◽  
H. Hayashi ◽  
T. Fujiwara ◽  
...  

2000 ◽  
Vol 28 (6) ◽  
pp. 762-765 ◽  
Author(s):  
P. R. Lange ◽  
I. Graham

To isolate mutants in the process of lipid mobilization during post-germinative growth we employed a screen using the pro-herbicide 2,4-dichlorophenoxybutyric acid (2,4-DB). The phenotypes of a number of 2,4-DB-resistant mutants are compared with previously characterized mutants disrupted in β-oxidation or the glyoxylate cycle. We conclude that the strength of 2,4-DB resistance and the ability of the seedlings to grow in the absence of exogenous sugar are inversely correlated. Sugar dependence of 2,4-DB-resistant seedlings is a consequence of impaired storage-lipid mobilization.


2005 ◽  
Vol 125 (1) ◽  
pp. 95-105 ◽  
Author(s):  
Motoko Awazuhara ◽  
Toru Fujiwara ◽  
Hiroaki Hayashi ◽  
Akiko Watanabe-Takahashi ◽  
Hideki Takahashi ◽  
...  

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Lie Wang ◽  
Kehan Chen ◽  
Ming Zhou

AbstractPlant sulfate transporters (SULTR) mediate absorption and distribution of sulfate (SO42−) and are essential for plant growth; however, our understanding of their structures and functions remains inadequate. Here we present the structure of a SULTR from Arabidopsis thaliana, AtSULTR4;1, in complex with SO42− at an overall resolution of 2.8 Å. AtSULTR4;1 forms a homodimer and has a structural fold typical of the SLC26 family of anion transporters. The bound SO42− is coordinated by side-chain hydroxyls and backbone amides, and further stabilized electrostatically by the conserved Arg393 and two helix dipoles. Proton and SO42− are co-transported by AtSULTR4;1 and a proton gradient significantly enhances SO42− transport. Glu347, which is ~7 Å from the bound SO42−, is required for H+-driven transport. The cytosolic STAS domain interacts with transmembrane domains, and deletion of the STAS domain or mutations to the interface compromises dimer formation and reduces SO42− transport, suggesting a regulatory function of the STAS domain.


Plants ◽  
2019 ◽  
Vol 8 (4) ◽  
pp. 95 ◽  
Author(s):  
Tomomi Morikawa-Ichinose ◽  
Sun-Ju Kim ◽  
Alaa Allahham ◽  
Ryota Kawaguchi ◽  
Akiko Maruyama-Nakashita

Plants take up sulfur (S), an essential element for all organisms, as sulfate, which is mainly attributed to the function of SULTR1;2 in Arabidopsis. A disruption mutant of SULTR1;2, sel1-10, has been characterized with phenotypes similar to plants grown under sulfur deficiency (−S). Although the effects of −S on S metabolism were well investigated in seedlings, no studies have been performed on mature Arabidopsis plants. To study further the effects of −S on S metabolism, we analyzed the accumulation and distribution of S-containing compounds in different parts of mature sel1-10 and of the wild-type (WT) plants grown under long-day conditions. While the levels of sulfate, cysteine, and glutathione were almost similar between sel1-10 and WT, levels of glucosinolates (GSLs) differed between them depending on the parts of the plant. GSLs levels in the leaves and stems were generally lower in sel1-10 than those in WT. However, sel1-10 seeds maintained similar levels of aliphatic GSLs to those in WT plants. GSL accumulation in reproductive tissues is likely to be prioritized even when sulfate supply is limited in sel1-10 for its role in S storage and plant defense.


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