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Article

A Novel Lysophosphatidic Acid Acyltransferase of Escherichia coli Produces Membrane Phospholipids with a cis-vaccenoyl Group and Is Related to Flagellar Formation

1
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan
2
Department of Biotechnology, College of Life Sciences, Ritsumeikan University, 1-1-1 Noji-higashi, Kusatsu, Shiga 525-8577, Japan
*
Author to whom correspondence should be addressed.
Biomolecules 2020, 10(5), 745; https://doi.org/10.3390/biom10050745
Received: 26 March 2020 / Revised: 2 May 2020 / Accepted: 7 May 2020 / Published: 11 May 2020
(This article belongs to the Special Issue Perspectives on Bacterial Flagellar Motor)
Lysophosphatidic acid acyltransferase (LPAAT) introduces fatty acyl groups into the sn-2 position of membrane phospholipids (PLs). Various bacteria produce multiple LPAATs, whereas it is believed that Escherichia coli produces only one essential LPAAT homolog, PlsC—the deletion of which is lethal. However, we found that E. coli possesses another LPAAT homolog named YihG. Here, we show that overexpression of YihG in E. coli carrying a temperature-sensitive mutation in plsC allowed its growth at non-permissive temperatures. Analysis of the fatty acyl composition of PLs from the yihG-deletion mutant (∆yihG) revealed that endogenous YihG introduces the cis-vaccenoyl group into the sn-2 position of PLs. Loss of YihG did not affect cell growth or morphology, but ∆yihG cells swam well in liquid medium in contrast to wild-type cells. Immunoblot analysis showed that FliC was highly expressed in ∆yihG cells, and this phenotype was suppressed by expression of recombinant YihG in ∆yihG cells. Transmission electron microscopy confirmed that the flagellar structure was observed only in ∆yihG cells. These results suggest that YihG has specific functions related to flagellar formation through modulation of the fatty acyl composition of membrane PLs. View Full-Text
Keywords: lysophosphatidic acid acyltransferase; membrane phospholipid diversity; swimming motility; flagellar formation lysophosphatidic acid acyltransferase; membrane phospholipid diversity; swimming motility; flagellar formation
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MDPI and ACS Style

Toyotake, Y.; Nishiyama, M.; Yokoyama, F.; Ogawa, T.; Kawamoto, J.; Kurihara, T. A Novel Lysophosphatidic Acid Acyltransferase of Escherichia coli Produces Membrane Phospholipids with a cis-vaccenoyl Group and Is Related to Flagellar Formation. Biomolecules 2020, 10, 745. https://doi.org/10.3390/biom10050745

AMA Style

Toyotake Y, Nishiyama M, Yokoyama F, Ogawa T, Kawamoto J, Kurihara T. A Novel Lysophosphatidic Acid Acyltransferase of Escherichia coli Produces Membrane Phospholipids with a cis-vaccenoyl Group and Is Related to Flagellar Formation. Biomolecules. 2020; 10(5):745. https://doi.org/10.3390/biom10050745

Chicago/Turabian Style

Toyotake, Yosuke, Masayoshi Nishiyama, Fumiaki Yokoyama, Takuya Ogawa, Jun Kawamoto, and Tatsuo Kurihara. 2020. "A Novel Lysophosphatidic Acid Acyltransferase of Escherichia coli Produces Membrane Phospholipids with a cis-vaccenoyl Group and Is Related to Flagellar Formation" Biomolecules 10, no. 5: 745. https://doi.org/10.3390/biom10050745

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