Self-Incompatibility in Papaver rhoeas Activates Nonspecific Cation Conductance Permeable to Ca2+ and K+[W]
Self-Incompatibility in Papaver rhoeas Activates Nonspecific Cation Conductance Permeable to Ca2+ and K+[W]
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DOI:
10.1104/pp.110.161927
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发表时间:
2010-12
期刊:
影响因子:
7.4
通讯作者:
Juyou Wu;Su-yang Wang;Yuchun Gu;Shaoling Zhang;S. Publicover;V. Franklin-Tong
中科院分区:
文献类型:
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作者:
Juyou Wu;Su-yang Wang;Yuchun Gu;Shaoling Zhang;S. Publicover;V. Franklin-Tong
Cellular responses rely on signaling. In plant cells, cytosolic free calcium is a major second messenger, and ion channels play a key role in mediating physiological responses. Self-incompatibility (SI) is an important genetically controlled mechanism to prevent self-fertilization. It uses interaction of matching S-determinants from the pistil and pollen to allow “self” recognition, which triggers rejection of incompatible pollen. In Papaver rhoeas, the S-determinants are PrsS and PrpS. PrsS is a small novel cysteine-rich protein; PrpS is a small novel transmembrane protein. Interaction of PrsS with incompatible pollen stimulates S-specific increases in cytosolic free calcium and alterations in the actin cytoskeleton, resulting in programmed cell death in incompatible but not compatible pollen. Here, we have used whole-cell patch clamping of pollen protoplasts to show that PrsS stimulates SI-specific activation of pollen grain plasma membrane conductance in incompatible but not compatible pollen grain protoplasts. The SI-activated conductance does not require voltage activation, but it is voltage sensitive. It is permeable to divalent cations (Ba2+ ≥ Ca2+ > Mg2+) and the monovalent ions K+ and NH4+ and is enhanced at voltages negative to −100 mV. The Ca2+ conductance is blocked by La3+ but not by verapamil; the K+ currents are tetraethylammonium chloride insensitive and do not require Ca2+. We propose that the SI-stimulated conductance may represent a nonspecific cation channel or possibly two conductances, permeable to monovalent and divalent cations. Our data provide insights into signal-response coupling involving a biologically important response. PrsS provides a rare example of a protein triggering alterations in ion channel activity.