| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2052645 | FEBS Letters | 2006 | 5 Pages |
Abstract
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.
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Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Yoshiki Yamaryo, Ken Motohashi, Ken-ichiro Takamiya, Toru Hisabori, Hiroyuki Ohta,