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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Horiuchi, Hiroyuki Kobayashi, Shingo Ohta, Akinori Mizuike, Aya Fukuda, Ryouichi |
| Description | Author Affiliation: Kobayashi S ( Department of Biotechnology, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.); Mizuike A ( Department of Biotechnology, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.); Horiuchi H ( Department of Biotechnology, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.); Fukuda R ( Department of Biotechnology, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.); Ohta A ( Department of Biotechnology, The University of Tokyo, 1-1-1, Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan. Electronic address: aaohta@isc.chubu.ac.jp.) |
| Abstract | In eukaryotic cells, phospholipids are synthesized exclusively in the defined organelles specific for each phospholipid species. To explain the reason for this compartmental specificity in the case of phosphatidylcholine (PC) synthesis, we constructed and characterized a Saccharomyces cerevisiae strain that lacked endogenous phosphatidylethanolamine (PE) methyltransferases but had a recombinant PE methyltransferase from Acetobacter aceti, which was fused with a mitochondrial targeting signal from yeast Pet100p and a 3 × HA epitope tag. This fusion protein, which we named as mitopmt, was determined to be localized to the mitochondria by fluorescence microscopy and subcellular fractionation. The expression of mitopmt suppressed the choline auxotrophy of a double deletion mutant of PEM1 and PEM2 (pem1Δpem2Δ) and enabled it to synthesize PC in the absence of choline. This growth suppression was observed even if the Kennedy pathway was inactivated by the repression of PCT1 encoding CTP:phosphocholine cytidylyltransferase, suggesting that PC synthesized in the mitochondria is distributed to other organelles without going through the salvage pathway. The pem1Δpem2Δ strain deleted for PSD1 encoding the mitochondrial phosphatidylserine decarboxylase was able to grow because of the expression of mitopmt in the presence of ethanolamine, implying that PE from other organelles, probably from the ER, was converted to PC by mitopmt. These results suggest that PC could move out of the mitochondria, and raise the possibility that its movement is not under strict directional limitations. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 9 |
| Volume Number | 1841 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2014-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Gene Expression Regulation, Fungal Mitochondria Genetics Phosphatidylcholines Biosynthesis Phosphatidylethanolamine N-Methyltransferase Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Acetobacter Chemistry Enzymology Bacterial Proteins Metabolism Carboxy-Lyases Deficiency Choline Choline-Phosphate Cytidylyltransferase Antagonists & Inhibitors Ethanolamine Genetic Complementation Test Isoenzymes Mitochondrial Proteins RNA, Small Interfering Recombinant Fusion Proteins Signal Transduction Transgenes Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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