ArticleThe Plant cell2012
Mitochondrial targeting of the Arabidopsis F1-ATPase γ-subunit via multiple compensatory and synergistic presequence motifs.
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 17 papers.
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Who cites it
17 citing papers in PubMed.
- Subcellular calcium dynamics and organelle perturbations in resistosome-mediated cell death.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Synthetic Biology of Plants and Microbes for Agriculture, Environment, and Future Applications.Chemical reviews · 2026Review
- Bamboo mosaic virus-induced metabolic reprogramming engages mitochondrial function to regulate redox homeostasis and defense responses in Nicotiana benthamiana.BMC plant biology · 2025Article
- A mitochondrial metalloprotease FtsH4 is required for symbiotic nitrogen fixation in Lotus japonicus nodules.Scientific reports · 2024Article
- Bilirubin Distribution in Plants at the Subcellular and Tissue Levels.Plant & cell physiology · 2024Article
- The structural components of the Azotobacter vinelandii iron-only nitrogenase, AnfDKG, form a protein complex within the plant mitochondrial matrix.Plant molecular biology · 2023Article
- An Interplay between Mitochondrial and ER Targeting of a Bacterial Signal Peptide in Plants.Plants (Basel, Switzerland) · 2023Article
- GREEN FLUORESCENT PROTEIN variants with enhanced folding are more efficiently imported into chloroplasts.Plant physiology · 2022Article
- On the nature of thiamine triphosphate in Arabidopsis.Plant direct · 2020Article
- Recognition motifs rather than phylogenetic origin influence the ability of targeting peptides to import nuclear-encoded recombinant proteins into rice mitochondria.Transgenic research · 2020Article
- A Synthetic Biology Workflow Reveals Variation in Processing and Solubility of Nitrogenase Proteins Targeted to Plant Mitochondria, and Differing Tolerance of Targeting Sequences in a Bacterial Nitrogenase Assay.Frontiers in plant science · 2020Article
- Cross-Species Functional Conservation and Possible Origin of the N-Terminal Specificity Domain of Mitochondrial Presequences.Frontiers in plant science · 2020Article
- Evolution and Design Principles of the Diverse Chloroplast Transit Peptides.Molecules and cells · 2018Review
- Fusion of a highly N-glycosylated polypeptide increases the expression of ER-localized proteins in plants.Scientific reports · 2018Article
- Transformation of nad7 into the nuclear genome rescues the slow growth3 mutant in Arabidopsis.RNA biology · 2018Article
- Expression of 16 Nitrogenase Proteins within the Plant Mitochondrial Matrix.Frontiers in plant science · 2017Article
- Once for All: A Novel Robust System for Co-expression of Multiple Chimeric Fluorescent Fusion Proteins in Plants.Frontiers in plant science · 2017Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of mitochondrial proteins are encoded in the nuclear genome and imported into mitochondria posttranslationally from the cytosol. An N-terminal presequence functions as the signal for the import of mitochondrial proteins. However, the functional information in the presequence remains elusive. This study reports the identification of critical sequence motifs from the presequence of Arabidopsis thaliana F1-ATPase γ-subunit (pFAγ). pFAγ was divided into six 10-amino acid segments, designated P1 to P6 from the N to the C terminus, each of which was further divided into two 5-amino acid subdivisions. These P segments and their subdivisions were substituted with Ala residues and fused to green fluorescent protein (GFP). Protoplast targeting experiments using these GFP constructs revealed that pFAγ contains several functional sequence motifs that are dispersed throughout the presequence. The sequence motifs DQEEG (P4a) and VVRNR (P5b) were involved in translocation across the mitochondrial membranes. The sequence motifs IAARP (P2b) and IAAIR (P3a) participated in binding to mitochondria. The sequence motifs RLLPS (P2a) and SISTQ (P5a) assisted in pulling proteins into the matrix, and the sequence motif IAARP (P2b) functioned in Tom20-dependent import. In addition, these sequence motifs exhibit complex relationships, including synergistic functions. Thus, multiple sequence motifs dispersed throughout the presequence are proposed to function cooperatively during protein import into mitochondria.
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