Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 283, Issue 36, Pages 24608-24616Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M803869200
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- CNRS
- UPMC Universite Paris 6
- Universite Paris-Diderot
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We recently characterized a novel heme biogenesis pathway required for heme c(i)' covalent binding to cytochrome b(6) in Chlamydomonas named system IV or CCB (cofactor assembly, complex C (b(6)f), subunit B (PetB)). To find out whether this CCB pathway also operates in higher plants and extend the knowledge of the c-type cytochrome biogenesis, we studied Arabidopsis insertion mutants in the orthologs of the CCB genes. The ccb1, ccb2, and ccb4 mutants show a phenotype characterized by a deficiency in the accumulation of the subunits of the cytochrome b(6)f complex and lack covalent heme binding to cytochrome b(6). These mutants were functionally complemented with the corresponding wild type cDNAs. Using fluorescent protein reporters, we demonstrated that the CCB1, CCB2, CCB3, and CCB4 proteins are targeted to the chloroplast compartment of Arabidopsis. We have extended our study to the YGGT family, to which CCB3 belongs, by studying insertion mutants of two additional members of this family for which no mutants were previously characterized, and we showed that they are not functionally involved in the CCB system. Thus, we demonstrate the ubiquity of the CCB proteins in chloroplast heme c(i)' binding.
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