RRC ID 66195
著者 Toyotake Y, Nishiyama M, Yokoyama F, Ogawa T, Kawamoto J, Kurihara T.
タイトル A Novel Lysophosphatidic Acid Acyltransferase of Escherichia coli Produces Membrane Phospholipids with a cis-vaccenoyl Group and Is Related to Flagellar Formation.
ジャーナル Biomolecules
Abstract 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.
巻・号 10(5)
公開日 2020-5-11
DOI 10.3390/biom10050745
PII biom10050745
PMID 32403425
PMC PMC7277886
MeSH Acyltransferases / metabolism* Escherichia coli / enzymology* Escherichia coli / growth & development Escherichia coli / ultrastructure Escherichia coli Proteins / metabolism* Flagella / metabolism* Flagella / ultrastructure Membrane Lipids / metabolism* Mutation / genetics Phospholipids / metabolism* Substrate Specificity Temperature
IF 4.082
リソース情報
原核生物(大腸菌) ME9062