Open AccessMetabolic compartmentation of plastid prenyllipid biosynthesis
Author(s) -
Keller Yves,
Bouvier Florence,
d'Harlingue Alain,
Camara Bilal
Publication year - 1998
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1998.2510413.x
Subject(s) - plastid , chloroplast , biochemistry , reductase , biology , complementary dna , biosynthesis , enzyme , gene
The addition of phytyl side chain to chlorophylls, tocopherols and phylloquinone is prerequisite to their integration into plastid membranes. We have cloned a cDNA encoding a pre‐geranylgeranyl reductase from Arabidopsis thaliana . The deduced primary structure predicts a mature size with a molecular mass of 47 kDa and displays a characteristic dinucleotide binding domain. Geranylgeranyl reductase expressed in Escherichia coli sequentially catalyzes the reduction of geranylgeranyl‐chlorophyll a into phytyl‐chlorophyll a as well as the reduction of free geranylgeranyl diphosphate into phytyl diphosphate. Due to its multifunctionality and weak hydrophobicity, we suggest that in plastid the same geranylgeranyl reductase is recruited into the chlorophyll, the tocopherol and the phylloquinone pathways. The geranylgeranyl reductase gene is up‐regulated during etioplast to chloroplast and chloroplast to chromoplast development.