ArticleThe Plant cell2004
Functional specialization amongst the Arabidopsis Toc159 family of chloroplast protein import receptors.
Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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Who cites it
97 citing papers in PubMed.
- Causes and consequences of cytonuclear incompatibility in hybrids of flowering plants.Journal of experimental botany · 2026Review
- Assembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts.Nature communications · 2026Article
- Identification, cloning and expression analysis of chloroplast TOC-TIC complex components in a CBMC plant biology · 2026Article
- Evolution of Plant AIG1-like Proteins: Different Modes of Sequence Divergence and Their Contributions to Functional Diversification.Plants (Basel, Switzerland) · 2026Article
- Integrated genomic and transcriptomic analysis reveals the mechanisms underlying leaf variegation in 'Gonggan' mandarin.BMC plant biology · 2025Article
- A viral protein targets mitochondria and chloroplasts by subverting general import pathways and specific receptors.Journal of virology · 2023Article
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- Probing the physiological role of the plastid outer-envelope membrane using the oemiR plasmid collection.G3 (Bethesda, Md.) · 2023Article
- Chloroplast protein translocation pathways and ubiquitin-dependent regulation at a glance.Journal of cell science · 2023Article
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- Multi-Knock-a multi-targeted genome-scale CRISPR toolbox to overcome functional redundancy in plants.Nature plants · 2023Article
- Low-Speed Clinorotation ofInternational journal of molecular sciences · 2023Article
- Chloroplast proteostasis: A story of birth, life, and death.Plant communications · 2023Review
- The journey of preproteins across the chloroplast membrane systems.Frontiers in physiology · 2023Review
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- Split-Ubiquitin Two-Hybrid Screen for Proteins Interacting with slToc159-1 and slToc159-2, Two Chloroplast Preprotein Import Receptors in Tomato (Plants (Basel, Switzerland) · 2022Article
- Mutations in the chloroplast inner envelope protein TIC100 impair and repair chloroplast protein import and impact retrograde signaling.The Plant cell · 2022Article
- Chloroplasts Protein Quality Control and Turnover: A Multitude of Mechanisms.International journal of molecular sciences · 2022Review
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- Molecular characterization, targeting and expression analysis of chloroplast and mitochondrion protein import components inFrontiers in plant science · 2022Article
37 more citing papers are in PubMed but not listed here.
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11 authors.
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Abstract
The initial stages of preprotein import into chloroplasts are mediated by the receptor GTPase Toc159. In Arabidopsis thaliana, Toc159 is encoded by a small gene family: atTOC159, atTOC132, atTOC120, and atTOC90. Phylogenetic analysis suggested that at least two distinct Toc159 subtypes, characterized by atToc159 and atToc132/atToc120, exist in plants. atTOC159 was strongly expressed in young, photosynthetic tissues, whereas atTOC132 and atTOC120 were expressed at a uniformly low level and so were relatively prominent in nonphotosynthetic tissues. Based on the albino phenotype of its knockout mutant, atToc159 was previously proposed to be a receptor with specificity for photosynthetic preproteins. To elucidate the roles of the other isoforms, we characterized Arabidopsis knockout mutants for each one. None of the single mutants had strong visible phenotypes, but toc132 toc120 double homozygotes appeared similar to toc159, indicating redundancy between atToc132 and atToc120. Transgenic complementation studies confirmed this redundancy but revealed little functional overlap between atToc132/atToc120 and atToc159 or atToc90. Unlike toc159, toc132 toc120 caused structural abnormalities in root plastids. Furthermore, when proteomics and transcriptomics were used to compare toc132 with ppi1 (a receptor mutant that is specifically defective in the expression, import, and accumulation of photosynthetic proteins), major differences were observed, suggesting that atToc132 (and atToc120) has specificity for nonphotosynthetic proteins. When both atToc159 and the major isoform of the other subtype, atToc132, were absent, an embryo-lethal phenotype resulted, demonstrating the essential role of Toc159 in the import mechanism.
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