The predicted C-terminal β-barrel structure of TGD4 is weakly similar to proteins of the outer cell membrane of Gram-negative bacteria. Here, we show that, like TGD2, the TGD4 protein when fused to DsRED specifically binds phosphatidic acid (PtdOH).

2012年1月23日 · The TGD4 protein binds phosphatidic acid (PtdOH) in vitro. (a) Of all phospholipids tested, the Ds RED–TGD4–His protein binds specifically to PtdOH in the lipid overlay assay. An immunoblot is shown with proteins detected using His-tag antibodies.

The TGD4 gene encodes a protein that appears to be associated with the ER membranes. Mutant ER microsomes show a decreased transfer of lipids to isolated plastids consistent with in vivo labeling data, indicating a disruption of ER-to-plastid lipid transfer.

2013年2月1日 · TGD4 is a predicted β-barrel membrane protein (12, 13) embedded in the chloroplast outer envelope and, like TGD2, specifically binds PtdOH (14). Based on the current findings, it seems likely that the TGD proteins form a lipid transfer conduit to import PtdOH from the ER through the plastid envelopes.

2008年8月8日 · The TGD4 gene encodes a protein that appears to be associated with the ER membranes. Mutant ER microsomes show a decreased transfer of lipids to isolated plastids consistent with in vivo labeling data, indicating a disruption of ER-to-plastid lipid transfer.

2015年4月8日 · Several lipid processing enzymes (PC synthase, TGD4, TGD2, BnCLIP1) are detected at ER–chloroplast membrane junctions. Analysis of membrane topology and mechanism of activity of each lipid processing enzyme should help to understand how lipids are released/consumed on each side of the transfer site.

Here, we show that, like TGD2, the TGD4 protein when fused to DsRED specifically binds phosphatidic acid (PtdOH). As previously shown for tgd1 mutants, tgd4 mutants have elevated PtdOH content, probably in extraplastidic membranes.

2012年5月1日 · The results suggest that TGD4 is an integral dimeric β-barrel lipid transfer protein that binds PtdOH with its N terminus and contains dimerization domains at its C terminus. Chloroplast lipid transfer processes in Chlamydomonas reinhardtii involving a TRIGALACTOSYLDIACYLGLYCEROL 2 (TGD2) orthologue. The Plant journal : for …

2010年4月21日 · This question was addressed through the analysis of double mutants of tgd1-1 or tgd4-3 in genetic mutant backgrounds leading to a defect in lipid fatty acid desaturation either in the ER (fad2) or the plastid (fad6).

Here, we show that, like TGD2, the TGD4 protein when fused to Ds RED specifically binds phosphatidic acid (PtdOH). As previously shown for tgd1 mutants, tgd4 mutants have elevated PtdOH content, probably in extraplastidic membranes.