ArticleProceedings of the National Academy of Sciences of the United States of America2005
AtCCMH, an essential component of the c-type cytochrome maturation pathway in Arabidopsis mitochondria, interacts with apocytochrome c.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed, 88 citations in OpenAlex.
- Structural divergence and molecular adaptation ofFrontiers in plant science · 2026Article
- Comparative analyses of the organelle genomes inFrontiers in plant science · 2025Article
- Recurrent evolutionary switches of mitochondrial cytochrome c maturation systems in Archaeplastida.Nature communications · 2024Article
- Oxidation ofAntioxidants (Basel, Switzerland) · 2023Article
- The biogenesis and regulation of the plant oxidative phosphorylation system.Plant physiology · 2023Review
- An Archaea-specificeLife · 2022Article
- A Case of Gene Fragmentation in Plant Mitochondria Fixed by the Selection of a Compensatory Restorer of Fertility-Like PPR Gene.Molecular biology and evolution · 2021Article
- PPR-DYW Protein EMP17 Is Required for Mitochondrial RNA Editing, Complex III Biogenesis, and Seed Development in Maize.Frontiers in plant science · 2021Article
- The OXA2a Insertase of Arabidopsis Is Required for CytochromePlant physiology · 2020Article
- Characterization and Analysis of the Mitochondrial Genome of Common Bean (International journal of molecular sciences · 2020Article
- Mitochondrial small heat shock protein mediates seed germination via thermal sensing.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Erv1 of Arabidopsis thaliana can directly oxidize mitochondrial intermembrane space proteins in the absence of redox-active Mia40.BMC biology · 2017Article
- The thioreduction component CcmG confers efficiency and the heme ligation component CcmH ensures stereo-specificity during cytochromeThe Journal of biological chemistry · 2017Article
- The Reverse Transcriptase/RNA Maturase Protein MatR Is Required for the Splicing of Various Group II Introns in Brassicaceae Mitochondria.The Plant cell · 2016Article
- Mitochondrial Genome of Palpitomonas bilix: Derived Genome Structure and Ancestral System for Cytochrome c Maturation.Genome biology and evolution · 2016Article
- Disruption of the CYTOCHROME C OXIDASE DEFICIENT1 gene leads to cytochrome c oxidase depletion and reorchestrated respiratory metabolism in Arabidopsis.Plant physiology · 2014Article
- Cytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Biochimica et biophysica acta · 2014Review
- The CcmFH complex is the system I holocytochrome c synthetase: engineering cytochrome c maturation independent of CcmABCDE.Molecular microbiology · 2014Article
- Interaction of holoCcmE with CcmF in heme trafficking and cytochrome c biosynthesis.Journal of molecular biology · 2014Article
- Review
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8 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The maturation of c-type cytochromes requires the covalent ligation of the heme cofactor to reduced cysteines of the CXXCH motif of apocytochromes. In contrast to mitochondria of other eukaryotes, plant mitochondria follow a pathway close to that found in alpha- and gamma-proteobacteria. We identified a nuclear-encoded protein, AtCCMH, the Arabidopsis thaliana ortholog of bacterial CcmH/CycL proteins. In bacteria, CcmH and the thioredoxin CcmG are components of a periplasmic thio-reduction pathway proposed to maintain the apocytochrome c cysteines in a reduced state. AtCCMH is located exclusively in mitochondria. AtCCMH is an integral protein of the inner membrane with the conserved RCXXC motif facing the intermembrane space. Reduction assays show that the cysteine thiols in the RCXXC motif of AtCCMH can form a disulfide bond that can be reduced by enzymatic thiol reductants. A reduced form of AtCCMH can reduce the intra-disulfide bridge of a model peptide of apocytochrome c. When expressed in Escherichia coli, AtCCMH coimmunoprecipitates with the bacterial CcmF, a proposed component of the heme lyase. Blue-native PAGE of mitochondrial membrane complexes reveals the colocalization of AtCCMH and AtCcmF(N2) in a 500-kDa complex. Yeast two-hybrid assays show an interaction between the AtCCMH intermembrane space domain and A. thaliana apocytochrome c. A. thaliana ccmh/ccmh knockout plants show lethality at the torpedo stage of embryogenesis. Our results show that AtCCMH is an essential mitochondrial protein with characteristics consistent with its proposed apocytochrome c-reducing and heme lyase function.
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