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Phosphatidic Acid Counteracts S-RNase Signaling in Pollen by Stabilizing the Actin Cytoskeleton.
- Source :
-
Plant Cell . May2018, Vol. 30 Issue 5, p1023-1039. 17p. - Publication Year :
- 2018
-
Abstract
- S-RNase is the female determinant of self-incompatibility (SI) in pear (Pyrus bretschneideri). After translocation to the pollen tube, S-RNase degrades rRNA and induces pollen tube death in an S -haplotype-specific manner. In this study, we found that the actin cytoskeleton is a target of P. bretschneideri S-RNase (PbrS-RNase) and uncovered a mechanism that involves phosphatidic acid (PA) and protects the pollen tube from PbrS-RNase cytotoxicity. PbrS-RNase interacts directly with PbrActin1 in an S -haplotype-independent manner, causing the actin cytoskeleton to depolymerize and promoting programmed cell death in the self-incompatible pollen tube. Pro-156 of PbrS-RNase is essential for the PbrS-RNase-PbrActin1 interaction, and the actin cytoskeleton-depolymerizing function of PbrS-RNase does not require its RNase activity. PbrS-RNase cytotoxicity enhances the expression of phospholipase D (PbrPLDΔ1), resulting in increased PA levels in the incompatible pollen tube. PbrPLDΔ1-derived PA initially prevents depolymerization of the actin cytoskeleton elicited by PbrS-RNase and delays the SI signaling that leads to pollen tube death. This work provides insights into the orchestration of the S-RNase-based SI response, in which increased PA levels initially play a protective role in incompatible pollen, until sustained PbrS-RNase activity reaches the point of no return and pollen tube growth ceases. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 10404651
- Volume :
- 30
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Plant Cell
- Publication Type :
- Academic Journal
- Accession number :
- 158018696
- Full Text :
- https://doi.org/10.1105/tpc.18.00021