ArticleJournal of experimental botany2015
Identification of cleavage sites and substrate proteins for two mitochondrial intermediate peptidases in Arabidopsis thaliana.
Article in Journal of experimental botany, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 66 citations in OpenAlex.
- A single-amino-acid cleavage controls global mitochondrial complex integrity.Nature structural & molecular biology · 2026Article
- Papaver S-determinants trigger mitochondrially derived ROS production and disrupt energy metabolism in incompatible pollen tubes.The Plant cell · 2026Article
- OsDUF2488 acts synergistically with OsPrx1.1, regulates ROS metabolism and promotes dehydration tolerance in rice.Plant biotechnology journal · 2025Article
- Mitochondrial proteases and their roles in mitophagy in plants, animals, and yeast.Plant & cell physiology · 2025Review
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- Simple prerequisite of presequence for mitochondrial protein import in the unicellular red alga Cyanidioschyzon merolae.Journal of cell science · 2024Article
- Article
- The roles of plant proteases and protease inhibitors in drought response: a review.Frontiers in plant science · 2023Review
- Proteolytic regulation of mitochondrial oxidative phosphorylation components in plants.Biochemical Society transactions · 2022Review
- Protein Processing in Plant Mitochondria Compared to Yeast and Mammals.Frontiers in plant science · 2022Review
- Dissecting the molecular mechanisms of mitochondrial import and maturation of peroxiredoxins from yeast and mammalian cells.Biophysical reviews · 2021Review
- LC-MS Based Draft Map of theFrontiers in plant science · 2021Article
- Plant expression of NifD protein variants resistant to mitochondrial degradation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The Mouse Heart Mitochondria N Terminome Provides Insights into ClpXP-Mediated Proteolysis.Molecular & cellular proteomics : MCP · 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
- Structural Studies of Glutamate Dehydrogenase (Isoform 1) FromFrontiers in plant science · 2020Article
- New beginnings and new ends: methods for large-scale characterization of protein termini and their use in plant biology.Journal of experimental botany · 2019Review
- Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp. PCC6803.Doklady. Biochemistry and biophysics · 2018Article
- Trypanosomal mitochondrial intermediate peptidase does not behave as a classical mitochondrial processing peptidase.PloS one · 2018Article
- The Plastid and Mitochondrial Peptidase Network inThe Plant cell · 2017Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Most mitochondrial proteins contain an N-terminal targeting signal that is removed by specific proteases following import. In plant mitochondria, only mitochondrial processing peptidase (MPP) has been characterized to date. Therefore, we sought to determine the substrates and cleavage sites of the Arabidopsis thaliana homologues to the yeast Icp55 and Oct1 proteins, using the newly developed ChaFRADIC method for N-terminal protein sequencing. We identified 88 and seven putative substrates for Arabidopsis ICP55 and OCT1, respectively. It was determined that the Arabidopsis ICP55 contains an almost identical cleavage site to that of Icp55 from yeast. However, it can also remove a far greater range of amino acids. The OCT1 substrates from Arabidopsis displayed no consensus cleavage motif, and do not contain the classical -10R motif identified in other eukaryotes. Arabidopsis OCT1 can also cleave presequences independently, without the prior cleavage of MPP. It was concluded that while both OCT1 and ICP55 were probably acquired early on in the evolution of mitochondria, their substrate profiles and cleavage sites have either remained very similar or diverged completely.
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