A cotton gene encoding a plasma membrane aquaporin is involved in seedling development and in response to drought stress

Abstract Background Celery is a widely cultivated vegetable abundant in ascorbate (AsA), a natural plant antioxidant capable of scavenging free radicals generated by abiotic stress in plants. Ascorbate peroxidase (APX) is a plant antioxidant enzyme that is important in the synthesis of AsA and scavenging of excess hydrogen peroxide. However, the characteristics and functions of APX in celery remain unclear to date. Results In this study, a gene encoding APX was cloned from celery and named AgAPX1. The transcription level of the AgAPX1 gene was significantly upregulated under drought stress. AgAPX1 was expressed in Escherichia coli BL21 (DE3) and purified. The predicted molecular mass of rAgAPX1 was 33.16 kDa, which was verified by SDS-PAGE assay. The optimum pH and temperature for rAgAPX1 were 7.0 and 55 °C, respectively. Transgenic Arabidopsis hosting the AgAPX1 gene showed elevated AsA content, antioxidant capacity and drought resistance. Less decrease in net photosynthetic rate, chlorophyll content, and relative water content contributed to the high survival rate of transgenic Arabidopsis lines after drought. Conclusions The characteristics of APX in celery were different from that in other species. The enhanced drought resistance of overexpressing AgAPX1 in Arabidopsis may be achieved by increasing the accumulation of AsA, enhancing the activities of various antioxidant enzymes, and promoting stomatal closure. Our work provides new evidence to understand APX and its response mechanisms to drought stress in celery.

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Transcriptional regulation by glucose of the yeastPMA1 gene encoding the plasma membrane H+-ATPase

Yeast ◽

10.1002/yea.320091006 ◽

1993 ◽

Vol 9 (10) ◽

pp. 1075-1084 ◽

Cited By ~ 47

Author(s):

Rajini Rao ◽

Daniela Drummond-Barbosa ◽

Carolyn W. Slayman

Keyword(s):

Transcriptional Regulation ◽

Plasma Membrane ◽

Gene Encoding

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Molecular cloning of a plasma membrane aquaporin in Stipa purpurea , and exploration of its role in drought stress tolerance

Gene ◽

10.1016/j.gene.2018.04.056 ◽

2018 ◽

Vol 665 ◽

pp. 41-48 ◽

Cited By ~ 4

Author(s):

Qian Chen ◽

Shihai Yang ◽

Xiangxiang Kong ◽

Chuntao Wang ◽

Nan Xiang ◽

...

Keyword(s):

Plasma Membrane ◽

Drought Stress ◽

Stress Tolerance ◽

Molecular Cloning ◽

Drought Stress Tolerance ◽

Stipa Purpurea

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The plasma membrane NADPH oxidase OsRbohA plays a crucial role in developmental regulation and drought-stress response in rice

Physiologia Plantarum ◽

10.1111/ppl.12389 ◽

2015 ◽

Vol 156 (4) ◽

pp. 421-443 ◽

Cited By ~ 32

Author(s):

Xiang Wang ◽

Mao-Mao Zhang ◽

Ya-Jing Wang ◽

Yin-Tao Gao ◽

Ri Li ◽

...

Keyword(s):

Plasma Membrane ◽

Drought Stress ◽

Stress Response ◽

Nadph Oxidase ◽

Crucial Role ◽

Developmental Regulation

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Opposing effects of podocin on the gating of podocyte TRPC6 channels evoked by membrane stretch or diacylglycerol

AJP Cell Physiology ◽

10.1152/ajpcell.00095.2013 ◽

2013 ◽

Vol 305 (3) ◽

pp. C276-C289 ◽

Cited By ~ 63

Author(s):

Marc Anderson ◽

Eun Young Kim ◽

Henning Hagmann ◽

Thomas Benzing ◽

Stuart E. Dryer

Keyword(s):

Plasma Membrane ◽

Transient Receptor Potential ◽

Receptor Potential ◽

Stretch Activation ◽

Gain Of Function ◽

Gene Encoding ◽

Membrane Stretch ◽

Transient Receptor ◽

Opposing Effects ◽

Interfering Rna

Gain-of-function mutations in the transient receptor potential (TRP) cation channel subfamily C member 6 ( TRPC6) gene and mutations in the NPHS2 gene encoding podocin result in nephrotic syndromes. The purpose of this study was to determine the functional significance of biochemical interactions between these proteins. We observed that gating of TRPC6 channels in podocytes is markedly mechanosensitive and can be activated by hyposmotic stretch or indentation of the plasma membrane. Stretch activation of cationic currents was blocked by small interfering RNA knockdown of TRPC6, as well as by SKF-96365 or micromolar La3+. Stretch activation of podocyte TRPC6 persisted in the presence of inhibitors of phospholipase C (U-73122) and phospholipase A2 (ONO-RS-082). Robust stretch responses also persisted when recording electrodes contained guanosine 5′- O-(2-thiodiphosphate) at concentrations that completely suppressed responses to ANG II. Stretch responses were enhanced by cytochalasin D but were abolished by the peptide GsMTx4, suggesting that forces are transmitted to the channels through the plasma membrane. Podocin and TRPC6 interact at their respective COOH termini. Knockdown of podocin markedly increased stretch-evoked activation of TRPC6 but nearly abolished TRPC6 activation evoked by a diacylglycerol analog. These data suggest that podocin acts as a switch to determine the preferred mode of TRPC6 activation. They also suggest that podocin deficiencies will result in Ca2+ overload in foot processes, as with gain-of-function mutations in the TRPC6 gene. Finally, they suggest that mechanical activation of TRP family channels and the preferred mode of TRP channel activation may depend on whether members of the stomatin/prohibitin family of hairpin loop proteins are present.

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