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Serine Palmitoyltransferase, the First Step Enzyme in Sphingolipid Biosynthesis, Is Involved in Nonhost Resistance

January 2009 , Volume 22 , Number  1
Pages  31 - 38

Yoshihiro Takahashi,1,2 Thomas Berberich,1 Hiroyuki Kanzaki,1 Hideo Matsumura,1 Hiromasa Saitoh,1 Tomonobu Kusano,2 and Ryohei Terauchi1,3

1Iwate Biotechnology Research Center, 22-174-4 Narita, Kitakami, Iwate 024-0003, Japan; 2Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba, Sendai, Miyagi 980-8577, Japan; 3Graduate School of Agricultural Sciences, Iwate University, 3-18-8 Ueda, Morioka, Iwate 020-8550, Japan

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Accepted 12 September 2008.

An overexpression screen of Nicotiana benthamiana cDNAs identified a gene for the LCB2 subunit of serine palmitoyltransferase (SPT) as a potent inducer of hypersensitive response-like cell death. The pyridoxal 5′-phosphate binding site of NbLCB2 is required for its function as a cell death inducer. NbLCB2 mRNA is accumulated after infection by nonhost pathogen Pseudomonas cichorii. Resistance of N. benthamiana against P. cichorii was compromised by treatment with an SPT inhibitor and in NbLCB2- and NbLCB1-silenced plants. These results suggest that biosynthesis of sphingolipids is necessary for the nonhost resistance of N. benthamiana against P. cichorii.

© 2009 The American Phytopathological Society