| Summary: | <p>Abstract</p> <p>Background</p> <p>The endoplasmic reticulum (ER) is a major signaling organelle, which integrates a variety of responses against physiological stresses. In plants, one such stress-integrating response is the N-rich protein (NRP)-mediated cell death signaling pathway, which is synergistically activated by combined ER stress and osmotic stress signals. Despite the potential of this integrated signaling to protect plant cells against different stress conditions, mechanistic knowledge of the pathway is lacking, and downstream components have yet to be identified.</p> <p>Results</p> <p>In the present investigation, we discovered an NAC domain-containing protein from soybean, GmNAC6 (<it>Glycine max </it>NAC6), to be a downstream component of the integrated pathway. Similar to <it>NRP-A </it>and <it>NRP-B, GmNAC6 </it>is induced by ER stress and osmotic stress individually, but requires both signals for full activation. Transient expression of <it>GmNAC6 </it>promoted cell death and hypersensitive-like responses <it>in planta</it>. <it>GmNAC6 </it>and <it>NRPs </it>also share overlapping responses to biotic signals, but the induction of <it>NRPs </it>peaked before the increased accumulation of GmNAC6 transcripts. Consistent with the delayed kinetics of <it>GmNAC6 </it>induction, increased levels of <it>NRP-A </it>and <it>NRP-B </it>transcripts induced promoter activation and the expression of the <it>GmNAC6 </it>gene.</p> <p>Conclusions</p> <p>Collectively, our results biochemically link GmNAC6 to the ER stress- and osmotic stress-integrating cell death response and show that GmNAC6 may act downstream of the NRPs.</p>
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