論文

査読有り 最終著者 責任著者 国際誌
2020年5月11日

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

Biomolecules
  • Yosuke Toyotake
  • ,
  • Masayoshi Nishiyama
  • ,
  • Fumiaki Yokoyama
  • ,
  • Takuya Ogawa
  • ,
  • Jun Kawamoto
  • ,
  • Tatsuo Kurihara

10
5
開始ページ
745
終了ページ
745
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.3390/biom10050745
出版者・発行元
MDPI AG

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.

リンク情報
DOI
https://doi.org/10.3390/biom10050745
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/32403425
PubMed Central
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7277886
URL
https://www.mdpi.com/2218-273X/10/5/745/pdf
ID情報
  • DOI : 10.3390/biom10050745
  • eISSN : 2218-273X
  • PubMed ID : 32403425
  • PubMed Central 記事ID : PMC7277886

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