ArticlePlant physiology2006
Functional characterization of sequence motifs in the transit peptide of Arabidopsis small subunit of rubisco.
Article in Plant physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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61 citing papers in PubMed.
- Loss of the plastidial hexokinase CsHXK3 triggers metabolic starvation and ROS imbalance leading to pollen abortion in cucumber.The Plant journal : for cell and molecular biology · 2026Article
- Evolutionary Refinement of Mitochondrial and Plastid Targeting Sequences Coincides with the Late Diversification of Land Plants.Molecular biology and evolution · 2025Article
- Genetically manipulated chloroplast stromal phosphate levels alter photosynthetic efficiency.Plant physiology · 2024Article
- Identification of a highly efficient chloroplast-targeting peptide for plastid engineering.PLoS biology · 2024Article
- The N-region sequence context impacts the chloroplast import efficiency of multi-TMD protein.Plant molecular biology · 2024Article
- Expression and localization of two β-carbonic anhydrases inFrontiers in plant science · 2024Article
- Compartmentalized Terpenoid Production in Plants Using Agrobacterium-Mediated Transient Expression.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Characterization of signal and transit peptides based on motif composition and taxon-specific patterns.Scientific reports · 2023Article
- Supplementing the Nuclear-Encoded PSII Subunit D1 Induces Dramatic Metabolic Reprogramming in Flag Leaves during Grain Filling in Rice.Plants (Basel, Switzerland) · 2023Article
- Salt stress-induced chloroplastic hydrogen peroxide stimulates pdTPI sulfenylation and methylglyoxal accumulation.The Plant cell · 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
- Differential contributions of two domains of NAI2 to the formation of the endoplasmic reticulum body.Frontiers in plant science · 2023Article
- GREEN FLUORESCENT PROTEIN variants with enhanced folding are more efficiently imported into chloroplasts.Plant physiology · 2022Article
- Pathway Engineering, Re-targeting, and Synthetic Scaffolding Improve the Production of Squalene in Plants.ACS synthetic biology · 2022Article
- Multigene manipulation of photosynthetic carbon metabolism enhances the photosynthetic capacity and biomass yield of cucumber under low-COFrontiers in plant science · 2022Article
- Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins.Frontiers in physiology · 2021Review
- A Thylakoid Membrane Protein Functions Synergistically with GUN5 in Chlorophyll Biosynthesis.Plant communications · 2020Article
- Nuclear-encoded synthesis of the D1 subunit of photosystem II increases photosynthetic efficiency and crop yield.Nature plants · 2020Article
- Tissue-Specific Regulation of Plastid Protein Import via Transit-Peptide Motifs.The Plant cell · 2020Article
1 more citing papers are in PubMed but not listed here.
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7 authors.
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Abstract
The transit peptides of nuclear-encoded chloroplast proteins are necessary and sufficient for targeting and import of proteins into chloroplasts. However, the sequence information encoded by transit peptides is not fully understood. In this study, we investigated sequence motifs in the transit peptide of the small subunit of the Rubisco complex by examining the ability of various mutant transit peptides to target green fluorescent protein reporter proteins to chloroplasts in Arabidopsis (Arabidopsis thaliana) leaf protoplasts. We divided the transit peptide into eight blocks (T1 through T8), each consisting of eight or 10 amino acids, and generated mutants that had alanine (Ala) substitutions or deletions, of one or two T blocks in the transit peptide. In addition, we generated mutants that had the original sequence partially restored in single- or double-T-block Ala (A) substitution mutants. Analysis of chloroplast import of these mutants revealed several interesting observations. Single-T-block mutations did not noticeably affect targeting efficiency, except in T1 and T4 mutations. However, double-T mutants, T2A/T4A, T3A/T6A, T3A/T7A, T4A/T6A, and T4A/T7A, caused a 50% to 100% loss in targeting ability. T3A/T6A and T4A/T6A mutants produced only precursor proteins, whereas T2A/T4A and T4A/T7A mutants produced only a 37-kD protein. Detailed analyses revealed that sequence motifs ML in T1, LKSSA in T3, FP and RK in T4, CMQVW in T6, and KKFET in T7 play important roles in chloroplast targeting. In T1, the hydrophobicity of ML is important for targeting. LKSSA in T3 is functionally equivalent to CMQVW in T6 and KKFET in T7. Furthermore, subcellular fractionation revealed that Ala substitution in T1, T3, and T6 produced soluble precursors, whereas Ala substitution in T4 and T7 produced intermediates that were tightly associated with membranes. These results demonstrate that the transit peptide contains multiple motifs and that some of them act in concert or synergistically.
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