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Chloroplasts play a crucial role in essential processes, such as photosynthesis and the synthesis of primary and diverse secondary metabolites. Recent studies have also highlighted their significance linked to phytohormone production in plant immunity, especially SA and JA. Ubiquitination, a key posttranslational modification, usually leads to target protein degradation, which acts as a signal for remodeling the proteome via the induction of protein endocytosis or targeting to other membrane associated systems. Previously, the potato E3 ligase StRFP1 was shown to enhance resistance against Phytophthora infestans, but its mechanism remained unclear. Here, we demonstrate that StRFP1 interacted with the dually localized plastid glucose 6-phosphate transporter StGPT1 on the endoplasmic reticulum (ER). Transiently expressed StGPT1-GFP located on the chloroplast and ER in plant cells. Overexpression of StGPT1enhances late blight resistance in potato and Nicotiana benthamiana, activates immune responses, including ROS bursts and up-regulation of PTI marker genes. The resistance function of StGPT1 seems to be related to its dual localization. Remarkably, StRFP1 ubiquitinates StGPT1 at the ER, possibly due to its merely transient function in peroxisomes, leading to apparent accumulation in chloroplasts. Our findings point to a novel mechanism by which a plant E3 ligase contributes to immunity via interacting with dually targeted GPT1 at the ER of plant cells.

Oomycete secretes a range of RxLR effectors into host cells to manipulate plant immunity by targeting proteins from several organelles. In this study, we report that chloroplast protein StFC-II is hijacked by a pathogen effector to enhance susceptibility. Phytophthora infestansRxLR effector Pi22922is activated during the early stages of P. infestanscolonization. Stable overexpression of Pi22922in plants suppresses flg22-triggered reactive oxygen species (ROS) burst and enhances leaf colonization by P. infestans. A potato ferrochelatase 2 (FC-II, a nuclear-encoded chloroplast-targeted protein), a key enzyme for heme biosynthesis in chloroplast, was identified as a target of Pi22922 in the cytoplasm. The pathogenicity of Pi22922 in plants is partially dependent on FC-II. Overexpression of StFC-IIdecreases resistance of potato and Nicotiana benthamianaagainst P. infestans, and silencing of NbFC-IIin N. benthamianareduces P. infestanscolonization.Overexpression of StFC-IIincreases heme content and reduces chlorophyll content and photosynthetic efficiency in potato leaves. Moreover, ROS accumulation both in chloroplast and cytoplasm is attenuated and defense-related genes are down-regulated in StFC-IIoverexpression transgenic potato and N. benthamianaleaves. Pi22922 inhibits E3 ubiquitin ligase StCHIP-mediated StFC-II degradation in the cytoplasm and promotes its accumulation in chloroplasts. In summary, this study characterizes a new mechanism that an oomycete RxLR effector suppresses host defenses by promoting StFC-II accumulation in chloroplasts, thereby compromising the host immunity and promoting susceptibility.