The LCB2 subunit of the sphingolip biosynthesis enzyme serine palmitoyltransferase can function as an attenuator of the hypersensitive response and Bax‐induced cell death

Abstract

Previous results showed that expression of the gene encoding the LONG-CHAIN BASE2 (LCB(2)) subunit of serine palmitoyltransferase (SPT), designated BcLCB(2), from nonheading Chinese cabbage (Brassica campestris ssp. chinensis) was up-regulated during hypersensitive cell death (HCD) induced by the Phytophthora boehmeriae elicitor PB90. Overexpression of BcLCB(2) in Nicotiana tabacum leaves suppressed the HCD normally initiated by elicitors and PB90-triggered H(2)O(2) accumulation. BcLCB(2) also functioned as a suppressor of mouse Bcl-2 associated X (Bax) protein-mediated HCD and cell death caused by Ralstonia solanacearum. BcLCB(2) overexpression suppressed Bax- and oxidant stress-triggered yeast cell death. Reactive oxygen species (ROS) accumulation induced by Bax was compromised in BcLCB(2)-overexpressing yeast cells. The findings that NbLCB(2) silencing in Nicotiana benthamiana enhanced elicitor-triggered HCD, combined with the fact that myriocin, a potent inhibitor of SPT, had no effect on Bax-induced programmed cell death, suggested that suppression of cell death was not involved in the dominant-negative effect that resulted from BcLCB(2) overexpression. A BcLCB(2) mutant assay showed that the suppression was not involved in SPT activity. The results suggest that plant HCD and stress-induced yeast cell death might share a common signal transduction pathway involving LCB(2), and that LCB(2) protects against cell death by inhibiting ROS accumulation, this inhibition being independent of SPT activity.