The rapeseed mitochondrial gene encoding a homologue of the bacterial protein Ccl1 is divided into two independently transcribed reading frames

Handa, Hirokazu; Bonnard, Géraldine; Grienenberger, Jean‐Michel

doi:10.1007/s004380050231

Cited by 11 publications

(11 citation statements)

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“…In contrast to the situation found in wheat and Oenothera berteriana (Schuster et al ., 1993; Gruska et al ., 1995), three genes encode proteins showing similarity with Ccl1 in the lower plant M. polymorpha (Oda et al ., 1992). In A. thaliana and rapeseed, the expression of a split ccl1N gene has been discussed (Handa et al ., 1996; Menassa et al ., 1997). A number of transmembrane domains can be predicted for the mitochondrial proteins, indicating a membrane topology similar to the bacterial Ccl1.…”

Section: System Imentioning

confidence: 99%

Mmicular mechanisms of cytochrome c biogenesis: three distinct systems

Kranz

Lill

Goldman

et al. 1998

Molecular Microbiology

261

299

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SummaryThe past 10 years have heralded remarkable progress in the understanding of the biogenesis of c-type cytochromes. The hallmark of c-type cytochrome synthesis is the covalent ligation of haem vinyl groups to two cysteinyl residues of the apocytochrome (at a CysXxx-Yyy-Cys-His signature motif). From genetic, genomic and biochemical studies, it is clear that three distinct systems have evolved in nature to assemble this ancient protein. In this review, common principles of assembly for all systems and the molecular mechanisms predicted for each system are summarized. Prokaryotes, plant mitochondria and chloroplasts use either system I or II, which are each predicted to use dedicated mechanisms for haem delivery, apocytochrome ushering and thioreduction. Accessory proteins of systems I and II co-ordinate the positioning of these two substrates at the membrane surface for covalent ligation. The third system has evolved specifically in mitochondria of fungi, invertebrates and vertebrates. For system III, a pivotal role is played by an enzyme called cytochrome c haem lyase (CCHL) in the mitochondrial intermembrane space.

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Section: System Imentioning

confidence: 99%

Mmicular mechanisms of cytochrome c biogenesis: three distinct systems

Kranz

Lill

Goldman

et al. 1998

Molecular Microbiology

261

299

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“…1). This protein is split into two ORFs in plant mitochondria, with the N-terminal half (ORF577) containing the most highly conserved residues, including the WWD domain (32). Interestingly, all residues that are conserved between the prokaryotic Ccl1 protein and eukaryotic ORF577 proteins are located in the large periplasmic domains P1, P2, and P3 (Fig.…”

Section: Proc Natl Acad Sci Usa 95 (1998)mentioning

confidence: 99%

Transmembrane heme delivery systems

Goldman

Beck

Monika

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

116

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Heme proteins play pivotal roles in a wealth of biological processes. Despite this, the molecular mechanisms by which heme traverses bilayer membranes for use in biosynthetic reactions are unknown. The biosynthesis of c-type cytochromes requires that heme is transported to the bacterial periplasm or mitochondrial intermembrane space where it is covalently ligated to two reduced cysteinyl residues of the apocytochrome. Results herein suggest that a family of integral membrane proteins in prokaryotes, protozoans, and plants act as transmembrane heme delivery systems for the biogenesis of c-type cytochromes. The complete topology of a representative from each of the three subfamilies was experimentally determined. Key histidinyl residues and a conserved tryptophan-rich region (designated the WWD domain) are positioned at the site of cytochrome c assembly for all three subfamilies. These histidinyl residues were shown to be essential for function in one of the subfamilies, an ABC transporter encoded by helABCD. We believe that a directed heme delivery pathway is vital for the synthesis of cytochromes c, whereby heme iron is protected from oxidation via ligation to histidinyl residues within the delivery proteins.

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“…In M. polymorpha, the part encoding the C-terminal end of ccmF is further split in 2 genes (40). In Brasicacea such as Arabidopsis the part encoding the N-terminal end of ccmF is encoded by 2 genes (41,42). Thus, the 3 Arabidopsis ccmF genes are named ccmF N1 , ccmF N2 , and ccmF C .…”

Section: Ccmf In Mitochondrial Genomes-mentioning

confidence: 99%

The Three Mitochondrial Encoded CcmF Proteins Form a Complex That Interacts with CCMH and c-Type Apocytochromes in Arabidopsis

Rayapuram¹,

Hagenmuller²,

Grienenberger

et al. 2008

Journal of Biological Chemistry

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Three reading frames called ccmF N1 , ccmF N2 , and ccmF c are found in the mitochondrial genome of Arabidopsis. These sequences are similar to regions of the bacterial gene ccmF involved in cytochrome c maturation. ccmF genes are always absent from animal and fungi genomes but are found in mitochondrial genomes of land plant and several evolutionary distant eukaryotes. In Arabidopsis, ccmF N2 despite the absence of a classical initiation codon is not a pseudo gene. The 3 ccmF genes of Arabidopsis are expressed at the protein level. Their products are integral proteins of the mitochondrial inner membrane with in total 11 to 13 predicted transmembrane helices. The conserved WWD domain of CcmF N2 is localized in the inter membrane space. The 3 CcmF proteins are all detected in a high molecular mass complex of 500 kDa by Blue Native PAGE. Direct interaction between CcmF N2 and both CcmF N1 and CcmF C is shown with the yeast two-hybrid split ubiquitin system, but no interaction is observed between CcmF N1 and CcmF C . Similarly, interaction is detected between CcmF N2 and apocytochrome c but also with apocytochrome c 1 . Finally, CcmF N1 and CcmF N2 both interact with CCMH previously shown to interact as well with cytochrome c. This strengthens the hypothesis that CcmF and CCMH make a complex that performs the assembly of heme with c-type apocytochromes in plant mitochondria.

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The rapeseed mitochondrial gene encoding a homologue of the bacterial protein Ccl1 is divided into two independently transcribed reading frames

Cited by 11 publications

References 0 publications

Mmicular mechanisms of cytochrome c biogenesis: three distinct systems

Mmicular mechanisms of cytochrome c biogenesis: three distinct systems

Transmembrane heme delivery systems

The Three Mitochondrial Encoded CcmF Proteins Form a Complex That Interacts with CCMH and c-Type Apocytochromes in Arabidopsis

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