Multiplicity of different cell- and organ-specific import routes for the NADPH-protochlorophyllide oxidoreductases A and B in plastids of Arabidopsis seedlings.
The NADPH-dependent protochlorophyllide (Pchlide) oxidoreductase (POR) is a photoenzyme that requires light for its catalytic activity and uses Pchlide itself as a photoreceptor. In Arabidopsis there are three PORs denoted PORA, PORB and PORC. The PORA and PORB genes are strongly expressed early in seedling development. In contrast to PORB the import of PORA into plastids of cotyledons is substrate-dependent and organ-specific. These differences in the import reactions between PORA and PORB most likely are due to different import mechanisms that are responsible for the uptake of these proteins. The two major core constituents of the translocon of the outer plastid envelope, Toc159 and Toc34, have been implicated in the binding and recognition of precursors of nuclear-encoded plastid proteins. Their involvement in conferring substrate dependency and organ specificity of PORA import was analyzed in intact Arabidopsis seedlings of wild type and the three mutants ppi3, ppi1 and ppi2 that are deficient in atToc34, atToc33, a closely related isoform of atToc34, and atToc159. Whereas none of these three Toc constituents is required for maintaining the organ specificity and substrate dependency of PORA import, atToc33 is indispensable for the import of PORB in cotyledons and true leaves suggesting that in these parts of the plant translocation of PORA and PORB occurs via two distinct import pathways. The analysis of PORA and PORB import into plastids of intact seedlings revealed an unexpected multiplicity of import routes that differed by their substrate, cell, tissue and organ specificities. This versatility of pathways for protein targeting to plastids suggests that in intact seedlings not only the constituents of the core complex of import channels but also other factors are involved in mediating the import of nuclear-encoded plastid proteins.
Kim
Chanhong
C
Institute of Plant Sciences, Plant Genetics, Swiss Federal Institute of Technology (ETH), CH-8092, Zurich, Switzerland.
Ham
Hyemin
H
Apel
Klaus
K
D017360:Arabidopsis / Q000201:enzymology* / Q000648:ultrastructure; D029681:Arabidopsis Proteins / Q000378:metabolism; D018548:Cotyledon / Q000378:metabolism / Q000648:ultrastructure; D009154:Mutation; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000378:metabolism*; D030821:Plants, Genetically Modified; D018087:Plastids / Q000201:enzymology*; D021381:Protein Transport / Q000502:physiology; D036226:Seedlings / Q000201:enzymology* / Q000648:ultrastructure
D029681:Arabidopsis Proteins; D044925:Oxidoreductases Acting on CH-CH Group Donors; C023886:protochlorophyllide reductase