ArticleThe Plant cell2012
A transit peptide-like sorting signal at the C terminus directs the Bienertia sinuspersici preprotein receptor Toc159 to the chloroplast outer membrane.
Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Identification, cloning and expression analysis of chloroplast TOC-TIC complex components in a CBMC plant biology · 2026Article
- A viral protein targets mitochondria and chloroplasts by subverting general import pathways and specific receptors.Journal of virology · 2023Article
- New Insights into the Chloroplast Outer Membrane Proteome and Associated Targeting Pathways.International journal of molecular sciences · 2022Review
- Molecular characterization, targeting and expression analysis of chloroplast and mitochondrion protein import components inFrontiers in plant science · 2022Article
- The ten amino acids of the oxygen-evolving enhancer of tobacco is sufficient as the peptide residues for protein transport to the chloroplast thylakoid.Plant molecular biology · 2021Article
- The rice white green leaf 2 gene causes defects in chloroplast development and affects the plastid ribosomal protein S9.Rice (New York, N.Y.) · 2018Article
- Transit peptide elements mediate selective protein targeting to two different types of chloroplasts in the single-cell C4 species Bienertia sinuspersici.Scientific reports · 2017Article
- Identification and in silico analysis of helical lipid binding regions in proteins belonging to the amphitropic protein family.Journal of biosciences · 2014Article
- Structural determinants allowing transferase activity in SENSITIVE TO FREEZING 2, classified as a family I glycosyl hydrolase.The Journal of biological chemistry · 2014Article
- One decade after the discovery of single-cell C4 species in terrestrial plants: what did we learn about the minimal requirements of C4 photosynthesis?Photosynthesis research · 2014Review
- Exploring mechanisms linked to differentiation and function of dimorphic chloroplasts in the single cell C4 species Bienertia sinuspersici.BMC plant biology · 2014Article
- The C-terminus of Bienertia sinuspersici Toc159 contains essential elements for its targeting and anchorage to the chloroplast outer membrane.Frontiers in plant science · 2014Article
- Targeting and assembly of components of the TOC protein import complex at the chloroplast outer envelope membrane.Frontiers in plant science · 2014Review
- Differential age-dependent import regulation by signal peptides.PLoS biology · 2012Article
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2 authors.
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Abstract
Although Toc159 is known to be one of the key GTPase receptors for selective recognition of chloroplast preproteins, the mechanism for its targeting to the chloroplast surface remains unclear. To compare the targeting of these GTPase receptors, we identified two Toc159 isoforms and a Toc34 from Bienertia sinuspersici, a single-cell C₄ species with dimorphic chloroplasts in individual chlorenchyma cells. Fluorescent protein tagging and immunogold studies revealed that the localization patterns of Toc159 were distinctive from those of Toc34, suggesting different targeting pathways. Bioinformatics analyses indicated that the C-terminal tails (CTs) of Toc159 possess physicochemical and structural properties of chloroplast transit peptides (cTPs). These results were further confirmed by fluorescent protein tagging, which showed the targeting of CT fusion proteins to the chloroplast surface. The CT of Bs Toc159 in reverse orientation functioned as a cleavable cTP that guided the fluorescent protein to the stroma. Moreover, a Bs Toc34 mutant protein was retargeted to the chloroplast envelope using the CTs of Toc159 or reverse sequences of other cTPs, suggesting their conserved functions. Together, our data show that the C terminus and the central GTPase domain represent a novel dual domain-mediated sorting mechanism that might account for the partitioning of Toc159 between the cytosol and the chloroplast envelope for preprotein recognition.
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