A mechanism implicating plastoglobules in thylakoid disassembly during senescence and nitrogen starvation

Plastoglobules are lipid droplets present in all plastid types. In chloroplasts, they are connected to the thylakoid membrane by the outer lipid half-bilayer. The plastoglobule core is composed of neutral lipids most prominently the prenylquinones, triacylglycerols, fatty acid phytyl esters but likely also unknown compounds. During stress and various developmental stages such as senescence, plastoglobule size and number increase due to the accumulation of lipids. However, their role is not limited to lipid storage. Indeed, the characterization of the plastoglobule proteome revealed the presence of enzymes. Importantly it has been demonstrated that these participate in isoprenoid lipid metabolic pathways at the plastoglobule, notably in the metabolism of prenylquinones. Recently, the characterization of two phytyl ester synthases has established a firm metabolic link between PG enzymatic activity and thylakoid disassembly during chloroplast senescence and nitrogen starvation

The Targeting of the atToc159 Preprotein Receptor to the Chloroplast Outer Membrane is Mediated by its GTPase Domain and is Regulated by GTP

The multimeric translocon at the outer envelope membrane of chloroplasts (Toc) initiates the recognition and import of nuclear-encoded preproteins into chloroplasts. Two Toc GTPases, Toc159 and Toc33/34, mediate preprotein recognition and regulate preprotein translocation. Although these two proteins account for the requirement of GTP hydrolysis for import, the functional significance of GTP binding and hydrolysis by either GTPase has not been defined. A recent study indicates that Toc159 is equally distributed between a soluble cytoplasmic form and a membrane-inserted form, raising the possibility that it might cycle between the cytoplasm and chloroplast as a soluble preprotein receptor. In the present study, we examined the mechanism of targeting and insertion of the Arabidopsis thaliana orthologue of Toc159, atToc159, to chloroplasts. Targeting of atToc159 to the outer envelope membrane is strictly dependent only on guanine nucleotides. Although GTP is not required for initial binding, the productive insertion and assembly of atToc159 into the Toc complex requires its intrinsic GTPase activity. Targeting is mediated by direct binding between the GTPase domain of atToc159 and the homologous GTPase domain of atToc33, the Arabidopsis Toc33/34 orthologue. Our findings demonstrate a role for the coordinate action of the Toc GTPases in assembly of the functional Toc complex at the chloroplast outer envelope membrane