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Published on January 24, 2008; 10.1104/pp.107.113506

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Received November 19, 2007
Accepted January 17, 2008

Serine palmitoyltransferase, a key enzyme for de novo synthesis of sphingolipids, is essential for male gametophyte development in Arabidopsis

Chong Teng , Haili Dong , Lihua Shi , Yan Deng , Jinye Mu , Jian Zhang , Xiaohui Yang , and Jianru Zuo *

State Key Laboratory of Plant Genomics and National Plant Gene Research Center (Beijing), Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China, and Graduate School, Chinese Academy of Sciences, Beijing 100049, China

* Corresponding author; email: jrzuo{at}genetics.ac.cn.

Sphingolipids are important signaling molecules involved in various cellular activities. De novo sphingolipid synthesis is initiated by a rate-limiting enzyme serine palmitoyltransferase (SPT), a heterodimer consisting of long-chain base1 (LCB1) and LCB2 subunits. A mutation in the Arabidopsis LCB1 gene, lcb1-1, was found to cause embryo lethality. However, the underpinning molecular and cellular mechanisms remain largely unclear. Here, we report the identification of the fumonisin B1 resistant11-2 (fbr11-2) mutant, an allele of lcb1-1. The fbr11-2 mutation, most likely an allele stronger than lcb1-1, was transmitted only through female gametophytes, and caused the formation of abortive microspores. During the second pollen mitosis, fbr11-2 initiated apoptotic cell death in binucleated microspores characteristic of nuclear DNA fragmentation, followed by cytoplasm shrinkage and organelle degeneration at the trinucleated stage. In addition, a double mutant with T-DNA insertions in two homologous LCB2 genes showed a phenotype similar to fbr11-2. Consistent with these observations, the FBR11/LCB1 expression was confined in microspores during microgametogenesis. These results suggest that SPT-modulated PCD plays an important role in the regulation of male gametophyte development.




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