ArticleThe Plant cell2012
Differential transit peptide recognition during preprotein binding and translocation into flowering plant plastids.
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 30 papers.
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Who cites it
30 citing papers in PubMed, 53 citations in OpenAlex.
- Single-molecule fluorescence and cross-linking reveal ligand-gated Toc34 oligomerization dynamics.Biophysical journal · 2026Article
- Converting antimicrobial into targeting peptides reveals key features governing protein import into mitochondria and chloroplasts.Plant communications · 2023Article
- Understanding protein import in diverse non-green plastids.Frontiers in genetics · 2023Review
- The journey of preproteins across the chloroplast membrane systems.Frontiers in physiology · 2023Review
- Transit Peptides Often Require Downstream Unstructured Sequence for Efficient Chloroplast Import inFrontiers in plant science · 2022Article
- Biosynthetic approaches to efficient assimilation of COFrontiers in bioengineering and biotechnology · 2022Review
- OsPPR939, a nad5 splicing factor, is essential for plant growth and pollen development in rice.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021Article
- Functional Organization of Sequence Motifs in Diverse Transit Peptides of Chloroplast Proteins.Frontiers in physiology · 2021Review
- Differential Evolution of α-Glucan Water Dikinase (GWD) in Plants.Plants (Basel, Switzerland) · 2020Article
- Evidence Supporting an Antimicrobial Origin of Targeting Peptides to Endosymbiotic Organelles.Cells · 2020Article
- Article
- PtomtAPX, a mitochondrial ascorbate peroxidase, plays an important role in maintaining the redox balance of Populus tomentosa Carr.Scientific reports · 2019Article
- Molecular Topology of the Transit Peptide during Chloroplast Protein Import.The Plant cell · 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
- Multiple Kinases Can Phosphorylate the N-Terminal Sequences of Mitochondrial Proteins inFrontiers in plant science · 2018Article
- The integration of chloroplast protein targeting with plant developmental and stress responses.BMC biology · 2017Review
- 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
- Chloroplast Hsp93 Directly Binds to Transit Peptides at an Early Stage of the Preprotein Import Process.Plant physiology · 2016Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite the availability of thousands of transit peptide (TP) primary sequences, the structural and/or physicochemical properties that determine TP recognition by components of the chloroplast translocon are not well understood. By combining a series of in vitro and in vivo experiments, we reveal that TP recognition is determined by sequence-independent interactions and vectorial-specific recognition domains. Using both native and reversed TPs for two well-studied precursors, small subunit of ribulose-1,5-bis-phosphate carboxylase/oxygenase, and ferredoxin, we exposed these two modes of recognition. Toc34 receptor (34-kD subunit of the translocon of the outer envelope) recognition in vitro, preprotein binding in organellar, precursor binding in vivo, and the recognition of TPs by the major stromal molecular motor Hsp70 are specific for the physicochemical properties of the TP. However, translocation in organellar and in vivo demonstrates strong specificity to recognition domain organization. This organization specificity correlates with the N-terminal placement of a strong Hsp70 recognition element. These results are discussed in light of how individual translocon components sequentially interact with the precursor during binding and translocation and helps explain the apparent lack of sequence conservation in chloroplast TPs.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.