ArticlePlant physiology2009
Multiple sequence motifs in the rubisco small subunit transit peptide independently contribute to Toc159-dependent import of proteins into chloroplasts.
Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- 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
- Identification of a highly efficient chloroplast-targeting peptide for plastid engineering.PLoS biology · 2024Article
- Converting antimicrobial into targeting peptides reveals key features governing protein import into mitochondria and chloroplasts.Plant communications · 2023Article
- GREEN FLUORESCENT PROTEIN variants with enhanced folding are more efficiently imported into chloroplasts.Plant physiology · 2022Article
- Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins.Frontiers in physiology · 2021Review
- Coevolution in Hybrid Genomes: Nuclear-Encoded Rubisco Small Subunits and Their Plastid-Targeting Translocons Accompanying Sequential Allopolyploidy Events in Triticum.Molecular biology and evolution · 2020Article
- Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants.Plants (Basel, Switzerland) · 2020Article
- On the nature of thiamine triphosphate in Arabidopsis.Plant direct · 2020Article
- Targeted delivery of nanomaterials with chemical cargoes in plants enabled by a biorecognition motif.Nature communications · 2020Article
- Tissue-Specific Regulation of Plastid Protein Import via Transit-Peptide Motifs.The Plant cell · 2020Article
- Transit Peptides From Photosynthesis-Related Proteins Mediate Import of a Marker Protein Into Different Plastid Types and Within Different Species.Frontiers in plant science · 2020Article
- Developmental regulation of protein import into plastids.Photosynthesis research · 2018Review
- GSPlant physiology · 2018Article
- Evolution and Design Principles of the Diverse Chloroplast Transit Peptides.Molecules and cells · 2018Review
- Prolines in Transit Peptides Are Crucial for Efficient Preprotein Translocation into Chloroplasts.Plant physiology · 2018Article
- Evolution of rubisco complex small subunit transit peptides from algae to plants.Scientific reports · 2017Article
- Transit peptide elements mediate selective protein targeting to two different types of chloroplasts in the single-cell C4 species Bienertia sinuspersici.Scientific reports · 2017Article
- Article
- Sequence Motifs in Transit Peptides Act as Independent Functional Units and Can Be Transferred to New Sequence Contexts.Plant physiology · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A large number of plastid proteins encoded by the nuclear genome are posttranslationally imported into plastids by at least two distinct mechanisms: the Toc159-dependent and Toc132/Toc120-dependent pathways. Light-induced photosynthetic proteins are imported through the Toc159-dependent pathway, whereas constitutive housekeeping plastid proteins are imported into plastids through the Toc132/Toc120 pathway. However, it remains unknown which features of the plastid protein transit peptide (TP) determine the import pathway. We have discovered sequence elements of the Rubisco small subunit TP (RbcS-tp) that play a role in determining import through the Toc159-dependent pathway in vivo. We generated multiple hybrid mutants using the RbcS-tp and the E1alpha-subunit of pyruvate dehydrogenase TP (E1alpha-tp) as representative peptides mediating import through the Toc159-dependent and Toc159-independent pathways, respectively. Import experiments using these hybrid mutants in wild-type and ppi2 mutant protoplasts revealed that multiple sequence motifs in the RbcS-tp independently contribute to Toc159-dependent protein import into chloroplasts. One of these motifs is the group of serine residues located in the N-terminal 12-amino acid segment and the other is the C-terminal T5 region of the RbcS-tp ranging from amino acid positions 41 to 49. Based on these findings, we propose that multiple sequence elements in the RbcS-tp contribute independently to Toc159-dependent import of proteins into chloroplasts.
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