ArticlePlant physiology2015
INTERMEDIATE CLEAVAGE PEPTIDASE55 Modifies Enzyme Amino Termini and Alters Protein Stability in Arabidopsis Mitochondria.
Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 38 citations in OpenAlex.
- A single-amino-acid cleavage controls global mitochondrial complex integrity.Nature structural & molecular biology · 2026Article
- 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
- Proteolytic regulation of mitochondrial oxidative phosphorylation components in plants.Biochemical Society transactions · 2022Review
- Genome-Wide Analysis of theInternational journal of molecular sciences · 2022Article
- Protein Processing in Plant Mitochondria Compared to Yeast and Mammals.Frontiers in plant science · 2022Review
- The Mouse Heart Mitochondria N Terminome Provides Insights into ClpXP-Mediated Proteolysis.Molecular & cellular proteomics : MCP · 2020Article
- Physiological and Proteomic Changes in the Apoplast Accompany Leaf Senescence inFrontiers in plant science · 2019Article
- Characterization of Aminopeptidase P from the Unicellular Cyanobacterium Synechocystis sp. PCC6803.Doklady. Biochemistry and biophysics · 2018Article
- Decoding the Divergent Subcellular Location of Two Highly Similar Paralogous LEA Proteins.International journal of molecular sciences · 2018Article
- Chloroplastic Serine Hydroxymethyltransferase FromFrontiers in plant science · 2018Article
- The Plastid and Mitochondrial Peptidase Network inThe Plant cell · 2017Review
- Structure of the human aminopeptidase XPNPEP3 and comparison of itsThe Journal of biological chemistry · 2017Article
- Protein Degradation Rate inThe Plant cell · 2017Article
- AtOMA1 Affects the OXPHOS System and Plant Growth in Contrast to Other Newly Identified ATP-Independent Proteases in Arabidopsis Mitochondria.Frontiers in plant science · 2017Article
- MIPEP recessive variants cause a syndrome of left ventricular non-compaction, hypotonia, and infantile death.Genome medicine · 2016Article
- The Arabidopsis Chloroplast Stromal N-Terminome: Complexities of Amino-Terminal Protein Maturation and Stability.Plant physiology · 2015Article
- Identification of protein N-termini in Cyanophora paradoxa cyanelles: transit peptide composition and sequence determinants for precursor maturation.Frontiers in plant science · 2015Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Precursor proteins containing mitochondrial peptide signals are cleaved after import by a mitochondrial processing peptidase. In yeast (Saccharomyces cerevisiae) and human (Homo sapiens), intermediate cleavage peptidase55 (ICP55) plays a role in stabilizing mitochondrial proteins by the removal of single amino acids from mitochondrial processing peptidase-processed proteins. We have investigated the role of a metallopeptidase (At1g09300) from Arabidopsis (Arabidopsis thaliana) that has sequence similarity to yeast ICP55. We identified this protein in mitochondria by mass spectrometry and have studied its function in a transfer DNA insertion line (icp55). Monitoring of amino-terminal peptides showed that Arabidopsis ICP55 was responsible for the removal of single amino acids, and its action explained the -3 arginine processing motif of a number of mitochondrial proteins. ICP55 also removed single amino acids from mitochondrial proteins known to be cleaved at nonconserved arginine sites, a subset of mitochondrial proteins specific to plants. Faster mitochondrial protein degradation rates not only for ICP55 cleaved protein but also for some non-ICP55 cleaved proteins were observed in Arabidopsis mitochondrial samples isolated from icp55 than from the wild type, indicating that a complicated protease degradation network has been affected. The lower protein stability of isolated mitochondria and the lack of processing of target proteins in icp55 were complemented by transformation with the full-length ICP55. Analysis of in vitro degradation rates and protein turnover rates in vivo of specific proteins indicated that serine hydroxymethyltransferase was affected in icp55. The maturation of serine hydroxymethyltransferase by ICP55 is unusual, as it involves breaking an amino-terminal diserine that is not known as an ICP55 substrate in other organisms and that is typically considered a sequence that stabilizes rather than destabilizes a protein.
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