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In vitro reconstitution of monogalactosyldiacylglycerol (MGDG) synthase regulation by thioredoxin
Author(s) -
Yamaryo Yoshiki,
Motohashi Ken,
Takamiya Ken-ichiro,
Hisabori Toru,
Ohta Hiroyuki
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.06.050
Subject(s) - thioredoxin , in vitro , chloroplast , biochemistry , escherichia coli , atp synthase , chemistry , chloroplast membrane , membrane , biology , enzyme , thylakoid , gene
Monogalactosyldiacylglycerol (MGDG), a major membrane lipid of chloroplasts, is synthesized by MGDG synthase (MGD) localized in chloroplast envelope membranes. We investigated whether MGD activity is regulated in a redox‐dependent manner using recombinant cucumber MGD overexpressed in Escherichia coli . We found that MGD activity is reversibly regulated by reduction and oxidation in vitro and that an intramolecular disulfide bond(s) is involved in MGD activation. Because thioredoxin efficiently reduced disulfide bonds to enhance MGD activity in vitro, MGD is potentially an envelope‐bound thioredoxin target protein in higher plants.