Open AccessSerine Palmitoyltransferase, the First Step Enzyme in Sphingolipid Biosynthesis, Is Involved in Nonhost Resistance
Author(s) -
Yoshihiro Takahashi,
Thomas Berberich,
Hiromitsu Kanzaki,
Hideo Matsumura,
Hiromasa Saitoh,
Tomonobu Kusano,
Ryohei Terauchi
Publication year - 2009
Publication title -
molecular plant-microbe interactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.565
H-Index - 153
eISSN - 1943-7706
pISSN - 0894-0282
DOI - 10.1094/mpmi-22-1-0031
Subject(s) - sphingolipid , biosynthesis , serine , enzyme , biochemistry , chemistry , microbiology and biotechnology , biology
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.