High impact information on AT2G30390

• Using RFLP analysis in recombinant inbred lines, the ferrochelatase-I gene was mapped to chromosome V and that for ferrochelatase-II to chromosome II [1].
• High levels of sucrose stimulated expression of ferrochelatase-I, but had no effect, or repressed slightly, the expression of the ferrochelatase-II isoform [1].
• Recently, however, mitochondrial targeting of ferrochelatase is being disputed since pea mitochondria appeared to accept a variety of chloroplast proteins including the type-1 ferrochelatase of Arabidopsis thaliana (L.) Heynh [2].
• By in vitro import assay with isolated pea (Pisum sativum L.) organelles, it has been proposed that one of two isoforms of ferrochelatase (type 1) is dual-targeted into both plastids and mitochondria, and functions for heme biosynthesis in the both organelles [2].
• Screening of a cucumber genomic or cDNA library did not allow any other ferrochelatase homologous gene to be isolated [2].

Biological context of AT2G30390

• The Arabidopsis thaliana genome has two genes (AtFC-I and AtFC-II), encoding ferrochelatase, the terminal enzyme of haem biosynthesis [3].

Anatomical context of AT2G30390

• Import experiments into isolated chloroplasts and mitochondria showed that the ferrochelatase-II gene encodes a precursor which is imported solely into the chloroplast, in contrast to ferrochelatase-I which is targeted to both organelles [1].
• Using in vitro import assays into purified mitochondria and chloroplasts we found that Arabidopsis ferrochelatase-I and ferrochelatase-II were not imported into mitochondria purified from Arabidopsis (or several other plants) but were imported into pea leaf chloroplasts [4].
• Clear evidence for the specific association of ferrochelatase protein with both thylakoid and envelope membranes has been obtained, thus suggesting strongly that the control of the branchpoint cannot be by spatial separation of the two chelatases [5].

Associations of AT2G30390 with chemical compounds

• It is widely believed that ferrochelatase (protoheme ferrolyase, EC 4.99.1.1), which catalyzes the insertion of ferrous ion into protoporphyrin IX to form protoheme, exists in both plastids and mitochondria of higher plants [2].

References