A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar Formation
Lysophosphatidic acid acyltransferase (LPAAT) introduces fatty acyl groups into the <i>sn</i>-2 position of membrane phospholipids (PLs). Various bacteria produce multiple LPAATs, whereas it is believed that <i>Escherichia coli</i> produces only one essential LPAAT homolog, P...
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MDPI AG
2020-05-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/10/5/745 |
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| author | Yosuke Toyotake Masayoshi Nishiyama Fumiaki Yokoyama Takuya Ogawa Jun Kawamoto Tatsuo Kurihara |
| author_facet | Yosuke Toyotake Masayoshi Nishiyama Fumiaki Yokoyama Takuya Ogawa Jun Kawamoto Tatsuo Kurihara |
| author_sort | Yosuke Toyotake |
| collection | DOAJ |
| description | Lysophosphatidic acid acyltransferase (LPAAT) introduces fatty acyl groups into the <i>sn</i>-2 position of membrane phospholipids (PLs). Various bacteria produce multiple LPAATs, whereas it is believed that <i>Escherichia coli</i> produces only one essential LPAAT homolog, PlsC—the deletion of which is lethal. However, we found that <i>E. coli</i> possesses another LPAAT homolog named YihG. Here, we show that overexpression of YihG in <i>E. coli</i> carrying a temperature-sensitive mutation in <i>plsC</i> allowed its growth at non-permissive temperatures. Analysis of the fatty acyl composition of PLs from the <i>yihG</i>-deletion mutant (∆<i>yihG</i>) revealed that endogenous YihG introduces the <i>cis</i>-vaccenoyl group into the <i>sn</i>-2 position of PLs. Loss of YihG did not affect cell growth or morphology, but ∆<i>yihG</i> cells swam well in liquid medium in contrast to wild-type cells. Immunoblot analysis showed that FliC was highly expressed in ∆<i>yihG</i> cells, and this phenotype was suppressed by expression of recombinant YihG in ∆<i>yihG</i> cells. Transmission electron microscopy confirmed that the flagellar structure was observed only in ∆<i>yihG</i> cells. These results suggest that YihG has specific functions related to flagellar formation through modulation of the fatty acyl composition of membrane PLs. |
| first_indexed | 2024-03-10T19:54:36Z |
| format | Article |
| id | doaj.art-82714de823f444a8b40e0b374bd62543 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-03-10T19:54:36Z |
| publishDate | 2020-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-82714de823f444a8b40e0b374bd625432023-11-20T00:06:41ZengMDPI AGBiomolecules2218-273X2020-05-0110574510.3390/biom10050745A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar FormationYosuke Toyotake0Masayoshi Nishiyama1Fumiaki Yokoyama2Takuya Ogawa3Jun Kawamoto4Tatsuo Kurihara5Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, JapanInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, JapanInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, JapanInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, JapanInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, JapanInstitute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, JapanLysophosphatidic acid acyltransferase (LPAAT) introduces fatty acyl groups into the <i>sn</i>-2 position of membrane phospholipids (PLs). Various bacteria produce multiple LPAATs, whereas it is believed that <i>Escherichia coli</i> produces only one essential LPAAT homolog, PlsC—the deletion of which is lethal. However, we found that <i>E. coli</i> possesses another LPAAT homolog named YihG. Here, we show that overexpression of YihG in <i>E. coli</i> carrying a temperature-sensitive mutation in <i>plsC</i> allowed its growth at non-permissive temperatures. Analysis of the fatty acyl composition of PLs from the <i>yihG</i>-deletion mutant (∆<i>yihG</i>) revealed that endogenous YihG introduces the <i>cis</i>-vaccenoyl group into the <i>sn</i>-2 position of PLs. Loss of YihG did not affect cell growth or morphology, but ∆<i>yihG</i> cells swam well in liquid medium in contrast to wild-type cells. Immunoblot analysis showed that FliC was highly expressed in ∆<i>yihG</i> cells, and this phenotype was suppressed by expression of recombinant YihG in ∆<i>yihG</i> cells. Transmission electron microscopy confirmed that the flagellar structure was observed only in ∆<i>yihG</i> cells. These results suggest that YihG has specific functions related to flagellar formation through modulation of the fatty acyl composition of membrane PLs.https://www.mdpi.com/2218-273X/10/5/745lysophosphatidic acid acyltransferasemembrane phospholipid diversityswimming motilityflagellar formation |
| spellingShingle | Yosuke Toyotake Masayoshi Nishiyama Fumiaki Yokoyama Takuya Ogawa Jun Kawamoto Tatsuo Kurihara A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar Formation Biomolecules lysophosphatidic acid acyltransferase membrane phospholipid diversity swimming motility flagellar formation |
| title | A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar Formation |
| title_full | A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar Formation |
| title_fullStr | A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar Formation |
| title_full_unstemmed | A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar Formation |
| title_short | A Novel Lysophosphatidic Acid Acyltransferase of <i>Escherichia coli</i> Produces Membrane Phospholipids with a <i>cis</i>-vaccenoyl Group and Is Related to Flagellar Formation |
| title_sort | novel lysophosphatidic acid acyltransferase of i escherichia coli i produces membrane phospholipids with a i cis i vaccenoyl group and is related to flagellar formation |
| topic | lysophosphatidic acid acyltransferase membrane phospholipid diversity swimming motility flagellar formation |
| url | https://www.mdpi.com/2218-273X/10/5/745 |
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