拟南芥
液泡
突变体
木质部
拟南芥
分区(防火)
生物化学
细胞生物学
钠氢反转运蛋白
互补
共转运蛋白
焦磷酸酶
生物
龙葵
化学
基因
植物
钠
运输机
细胞质
酶
有机化学
作者
Isabel Egea,Benito Pineda,Ana Ortíz‐Atienza,Félix Plasencia,Stéphanie Drevensek,Begoña García‐Sogo,Fernando J. Yuste‐Lisbona,Javier Barrero‐Gil,Alejandro Atarés,Francisco Pardo,Frédy Barneche,Trinidad Angosto,Carmen Capel,Julio Salinas,Wim H. Vriezen,Elisabeth Esch,Chris Bowler,María C. Bolarín,Vicente Moreno,Rafael Lozano
出处
期刊:Plant Physiology
[Oxford University Press]
日期:2017-12-11
卷期号:176 (2): 1676-1693
被引量:52
摘要
Characterization of a new tomato (Solanum lycopersicum) T-DNA mutant allowed for the isolation of the CALCINEURIN B-LIKE PROTEIN 10 (SlCBL10) gene whose lack of function was responsible for the severe alterations observed in the shoot apex and reproductive organs under salinity conditions. Physiological studies proved that SlCBL10 gene is required to maintain a proper low Na+/Ca2+ ratio in growing tissues allowing tomato growth under salt stress. Expression analysis of the main responsible genes for Na+ compartmentalization (i.e. Na+/H+ EXCHANGERs, SALT OVERLY SENSITIVE, HIGH-AFFINITY K+ TRANSPORTER 1;2, H+-pyrophosphatase AVP1 [SlAVP1] and V-ATPase [SlVHA-A1]) supported a reduced capacity to accumulate Na+ in Slcbl10 mutant leaves, which resulted in a lower uploading of Na+ from xylem, allowing the toxic ion to reach apex and flowers. Likewise, the tomato CATION EXCHANGER 1 and TWO-PORE CHANNEL 1 (SlTPC1), key genes for Ca2+ fluxes to the vacuole, showed abnormal expression in Slcbl10 plants indicating an impaired Ca2+ release from vacuole. Additionally, complementation assay revealed that SlCBL10 is a true ortholog of the Arabidopsis (Arabidopsis thaliana) CBL10 gene, supporting that the essential function of CBL10 is conserved in Arabidopsis and tomato. Together, the findings obtained in this study provide new insights into the function of SlCBL10 in salt stress tolerance. Thus, it is proposed that SlCBL10 mediates salt tolerance by regulating Na+ and Ca2+ fluxes in the vacuole, cooperating with the vacuolar cation channel SlTPC1 and the two vacuolar H+-pumps, SlAVP1 and SlVHA-A1, which in turn are revealed as potential targets of SlCBL10.
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