Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtii
Phosphatidylglycerol (PG) and cardiolipin (CL) are two essential classes of phospholipid in plants and algae. Phosphatidylglycerophosphate synthase (PGPS) and cardiolipin synthase (CLS) involved in the biosynthesis of PG and CL belong to CDP-alcohol phosphotransferase and share overall amino acid se...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-01-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01542/full |
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| author | Chun-Hsien eHung Koichi eKobayashi Hajime eWada Hajime eWada Yuki eNakamura Yuki eNakamura |
| author_facet | Chun-Hsien eHung Koichi eKobayashi Hajime eWada Hajime eWada Yuki eNakamura Yuki eNakamura |
| author_sort | Chun-Hsien eHung |
| collection | DOAJ |
| description | Phosphatidylglycerol (PG) and cardiolipin (CL) are two essential classes of phospholipid in plants and algae. Phosphatidylglycerophosphate synthase (PGPS) and cardiolipin synthase (CLS) involved in the biosynthesis of PG and CL belong to CDP-alcohol phosphotransferase and share overall amino acid sequence homology. However, it remains elusive whether PGPS and CLS are functionally distinct in vivo. Here, we report identification of a gene encoding CLS in Chlamydomonas reinhardtii, CrCLS1, and its functional compatibility. Whereas CrCLS1 did not complement the growth phenotype of a PGPS mutant of Synechocystis sp. PCC 6803, it rescued the temperature-sensitive growth phenotype, growth profile with different carbon sources, phospholipid composition and enzyme activity of ∆crd1, a CLS mutant of Saccharomyces cerevisiae. These results suggest that CrCLS1 encodes a functional CLS of C. reinhardtii as the first identified algal CLS, whose enzyme function is distinct from that of PGPSs from C. reinhardtii. Comparison of CDP-alcohol phosphotransferase motif between PGPS and CLS among different species revealed a possible additional motif that might define the substrate specificity of these closely related enzymes. |
| first_indexed | 2024-12-15T00:35:29Z |
| format | Article |
| id | doaj.art-ecac94f37dc1416c91567efc83d95850 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-15T00:35:29Z |
| publishDate | 2016-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-ecac94f37dc1416c91567efc83d958502022-12-21T22:41:49ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-01-01610.3389/fmicb.2015.01542172185Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtiiChun-Hsien eHung0Koichi eKobayashi1Hajime eWada2Hajime eWada3Yuki eNakamura4Yuki eNakamura5Institute of Plant and Microbial Biology, Academia SinicaThe University of TokyoThe University of TokyoJapan Science and Technology AgencyInstitute of Plant and Microbial Biology, Academia SinicaJapan Science and Technology AgencyPhosphatidylglycerol (PG) and cardiolipin (CL) are two essential classes of phospholipid in plants and algae. Phosphatidylglycerophosphate synthase (PGPS) and cardiolipin synthase (CLS) involved in the biosynthesis of PG and CL belong to CDP-alcohol phosphotransferase and share overall amino acid sequence homology. However, it remains elusive whether PGPS and CLS are functionally distinct in vivo. Here, we report identification of a gene encoding CLS in Chlamydomonas reinhardtii, CrCLS1, and its functional compatibility. Whereas CrCLS1 did not complement the growth phenotype of a PGPS mutant of Synechocystis sp. PCC 6803, it rescued the temperature-sensitive growth phenotype, growth profile with different carbon sources, phospholipid composition and enzyme activity of ∆crd1, a CLS mutant of Saccharomyces cerevisiae. These results suggest that CrCLS1 encodes a functional CLS of C. reinhardtii as the first identified algal CLS, whose enzyme function is distinct from that of PGPSs from C. reinhardtii. Comparison of CDP-alcohol phosphotransferase motif between PGPS and CLS among different species revealed a possible additional motif that might define the substrate specificity of these closely related enzymes.http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01542/fullChlamydomonas reinhardtiiSaccharomyces cerevisiaecardiolipinSynechocystis sp. PCC 6803PhosphatidylglycerolCardiolipin synthase |
| spellingShingle | Chun-Hsien eHung Koichi eKobayashi Hajime eWada Hajime eWada Yuki eNakamura Yuki eNakamura Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtii Frontiers in Microbiology Chlamydomonas reinhardtii Saccharomyces cerevisiae cardiolipin Synechocystis sp. PCC 6803 Phosphatidylglycerol Cardiolipin synthase |
| title | Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtii |
| title_full | Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtii |
| title_fullStr | Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtii |
| title_full_unstemmed | Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtii |
| title_short | Functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase CrCLS1 in Chlamydomonas reinhardtii |
| title_sort | functional specificity of cardiolipin synthase revealed by the identification of a cardiolipin synthase crcls1 in chlamydomonas reinhardtii |
| topic | Chlamydomonas reinhardtii Saccharomyces cerevisiae cardiolipin Synechocystis sp. PCC 6803 Phosphatidylglycerol Cardiolipin synthase |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2015.01542/full |
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