Location: Plant Gene Expression Center Albany_CA
Title: Tomato pistil factor STIG1 promotes in vivo pollen tube growth by binding to phosphatidylinositol 3-phosphate and the extracellular domain of the pollen receptor kinase LePRK2 Authors
|Huang, Wei-Jie -|
|Liu, Hai-Kuan -|
|Tang, Wei-Hua -|
Submitted to: The Plant Cell
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: May 28, 2014
Publication Date: June 17, 2014
Citation: Huang, W., Liu, H., McCormick, S.M., Tang, W. 2014. Tomato pistil factor STIG1 promotes in vivo pollen tube growth by binding to phosphatidylinositol 3-phosphate and the extracellular domain of the pollen receptor kinase LePRK2. The Plant Cell. DOI: 10.1105/tpc.114.123281. Interpretive Summary: A protein called STIGMA-SPECIFIC1 (STIG1), which is present in the female part of the flower, is important for pollen tube growth in tomato. Particular amino acids in this protein bind to a lipid called PI(3)P, while different amino acids interact with a pollen protein called POLLEN RECEPTOR KINASE2; these protein interactions underlie how STIG1 promotes pollen tube growth.
Technical Abstract: The speed of pollen tube growth is a major determinant of reproductive success in flowering plants. Tomato (Solanum lycopersicum) STIGMA-SPECIFIC PROTEIN1 (STIG1), a small Cys-rich protein from the pistil, was previously identified as a binding partner of the pollen receptor kinase LePRK2 and shown to promote pollen tube growth in vitro. However, the in vivo function of STIG1 and the underlying mechanism of its promotive effect were unknown. Here, we show that a 7-kD processed peptide of STIG1 is abundant in the stigmatic exudate and accumulates at the pollen tube surface, where it can bind LePRK2. AntisenseLePRK2 pollen was less responsive than wild-type pollen to exogenous STIG1 in an in vitro pollen germination assay. Silencing of STIG1 reduced both the in vivo pollen tube elongation rate and seed production. Using partial deletion and point mutation analyses, two regions underlying the promotive activity of the STIG1 processed peptide were identified: amino acids 80 to 83, which interact with LePRK2; and amino acids 88 to 115, which bind specifically to phosphatidylinositol 3-phosphate [PI(3)P]. Furthermore, exogenous STIG1 elevated the overall redox potential of pollen tubes in both PI(3)P-dependent and LePRK2-dependent manners. Our results demonstrate that STIG1 conveys growth-promoting signals acting through the pollen receptor kinase LePRK2, a process that relies on the external phosphoinositide PI(3)P.