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

Biomolecules ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 745
Author(s):  
Yosuke Toyotake ◽  
Masayoshi Nishiyama ◽  
Fumiaki Yokoyama ◽  
Takuya Ogawa ◽  
Jun Kawamoto ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lysophosphatidic Acid ◽  
Immunoblot Analysis ◽  
Fatty Acyl ◽  
Temperature Sensitive ◽  
Membrane Phospholipids ◽  
E Coli ◽  
Acyl Composition ◽  
Lysophosphatidic Acid Acyltransferase ◽  
Fatty Acyl Composition

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.

Effect of membrane fatty acyl composition on LDL metabolism in Hep G2 hepatocytes

Biochemistry ◽  
1990 ◽  
Vol 29 (28) ◽  
pp. 6626-6632 ◽  
Author(s):  
Paul Kuo ◽  
Mark Weinfeld ◽  
Joseph Loscalzo
Keyword(s):  
Fatty Acyl ◽  
Hep G2 ◽  
Acyl Composition ◽  
Fatty Acyl Composition

scholarly journals Enhanced Production of Fatty Acid Ethyl Ester with Engineered fabHDG Operon in Escherichia coli

2019 ◽  
Vol 7 (11) ◽  
pp. 552 ◽  
Author(s):  
Ziaur Rahman ◽  
Bong Hyun Sung ◽  
Javed Nawab ◽  
Muhammad Faisal Siddiqui ◽  
Abid Ali ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Ethyl Ester ◽  
Feedback Inhibition ◽  
Acid Ethyl Ester ◽  
Fatty Acid Ethyl Ester ◽  
Fatty Acyl ◽  
Dodecanoic Acid ◽  
E Coli ◽  
Enhanced Production

Biodiesel, or fatty acid ethyl ester (FAEE), is an environmentally safe, next-generation biofuel. Conventionally, FAEE is produced by the conversion of oil/fats, obtained from plants, animals, and microorganisms, by transesterification. Recently, metabolic engineering of bacteria for ready-to-use biodiesel was developed. In Escherichia coli, it is produced by fatty acyl-carrier proteins and ethanol, with the help of thioesterase (TesB) and wax synthase (WS) enzymes. One of the foremost barriers in microbial FAEE production is the feedback inhibition of the fatty acid (FA) operon (fabHDG). Here, we studied the effect of biodiesel biosynthesis in E. coli with an engineered fabHDG operon. With a basic FAEE producing BD1 strain harboring tes and ws genes, biodiesel of 32 mg/L were produced. Optimal FAEE biosynthesis was achieved in the BD2 strain that carries an overexpressed operon (fabH, fabD, and fabG genes) and achieved up to 1291 mg/L of biodiesel, a 40-fold rise compared to the BD1 strain. The composition of FAEE obtained from the BD2 strain was 65% (C10:C2, decanoic acid ethyl ester) and 35% (C12:C2, dodecanoic acid ethyl ester). Our findings indicate that overexpression of the native FA operon, along with FAEE biosynthesis enzymes, improved biodiesel biosynthesis in E. coli.

scholarly journals Genetic and Functional Analyses of the Conserved C-Terminal Core Domain of Escherichia coli FtsZ

1999 ◽  
Vol 181 (24) ◽  
pp. 7531-7544 ◽  
Author(s):  
Xiaolan Ma ◽  
William Margolin
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Immunoblot Analysis ◽  
Conserved Residues ◽  
Core Domain ◽  
Mutant Proteins ◽  
E Coli ◽  
Stable Mutant ◽  
Functional Analyses

ABSTRACT In Escherichia coli, FtsZ is required for the recruitment of the essential cell division proteins FtsA and ZipA to the septal ring. Several C-terminal deletions of E. coliFtsZ, including one of only 12 amino acids that removes the highly conserved C-terminal core domain, failed to complement chromosomalftsZ mutants when expressed on a plasmid. To identify key individual residues within the core domain, six highly conserved residues were replaced with alanines. All but one of these mutants (D373A) failed to complement an ftsZ chromosomal mutant. Immunoblot analysis demonstrated that whereas I374A and F377A proteins were unstable in the cell, L372A, D373A, P375A, and L378A proteins were synthesized at normal levels, suggesting that they were specifically defective in some aspect of FtsZ function. In addition, all four of the stable mutant proteins were able to localize and form rings at potential division sites in chromosomal ftsZ mutants, implying a defect in a function other than localization and multimerization. Because another proposed function of FtsZ is the recruitment of FtsA and ZipA, we tested whether the C-terminal core domain was important for interactions with these proteins. Using two different in vivo assays, we found that the 12-amino-acid truncation of FtsZ was defective in binding to FtsA. Furthermore, two point mutants in this region (L372A and P375A) showed weakened binding to FtsA. In contrast, ZipA was capable of binding to all four stable point mutants in the FtsZ C-terminal core but not to the 12-amino-acid deletion.

scholarly journals Role of Virulence Factors in Resistance of Avian Pathogenic Escherichia coli to Serum and in Pathogenicity

2003 ◽  
Vol 71 (1) ◽  
pp. 536-540 ◽  
Author(s):  
Melha Mellata ◽  
Maryvonne Dho-Moulin ◽  
Charles M. Dozois ◽  
Roy Curtiss ◽  
Peter K. Brown ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Virulence Factors ◽  
Bacterial Resistance ◽  
Serum Resistance ◽  
Temperature Sensitive ◽  
E Coli ◽  
Pathogenic Escherichia Coli ◽  
K1 Capsule

ABSTRACT In chickens, colibacillosis is caused by avian pathogenic Escherichia coli (APEC) via respiratory tract infection. Many virulence factors, including type 1 (F1A) and P (F11) fimbriae, curli, aerobactin, K1 capsule, and temperature-sensitive hemagglutinin (Tsh) and plasmid DNA regions have been associated with APEC. A strong correlation between serum resistance and virulence has been demonstrated, but roles of virulence factors in serum resistance have not been well elucidated. By using mutants of APEC strains TK3, MT78, and χ7122, which belong to serogroups O1, O2, and O78, respectively, we investigated the role of virulence factors in resistance to serum and pathogenicity in chickens. Our results showed that serum resistance is one of the pathogenicity mechanisms of APEC strains. Virulence factors that increased bacterial resistance to serum and colonization of internal organs of infected chickens were O78 lipopolysaccharide of E. coli χ7122 and the K1 capsule of E. coli MT78. In contrast, curli, type 1, and P fimbriae did not appear to contribute to serum resistance. We also showed that the iss gene, which was previously demonstrated to increase resistance to serum in certain E. coli strains, is located on plasmid pAPEC-1 of E. coli χ7122 but does not play a major role in resistance to serum for strain χ7122.

Altered phospholipid metabolism in pressure-overload hypertrophied hearts

1986 ◽  
Vol 250 (1) ◽  
pp. H1-H6 ◽  
Author(s):  
D. K. Reibel ◽  
B. O'Rourke ◽  
K. A. Foster ◽  
H. Hutchinson ◽  
C. E. Uboh ◽  
...  
Keyword(s):  
Linoleic Acid ◽  
Pressure Overload ◽  
Phospholipid Metabolism ◽  
Fatty Acyl ◽  
Membrane Function ◽  
Acyl Composition ◽  
Fatty Acyl Composition ◽  
Abdominal Aortic ◽  
Individual Phospholipid Class ◽  
The Individual

The content and fatty acyl composition of phospholipids were examined in pressure-overload hypertrophied hearts. Cardiac hypertrophy was induced in rats by abdominal aortic constriction. Twenty-one days postconstriction the content of myocardial phosphatidylcholine (PC), sphingomyelin, and phosphatidylinositol (PI) was significantly elevated by 10, 10, and 20%, respectively. The essential fatty acid, linoleic acid, was markedly reduced in PC, phosphatidylethanolamine (PE), PI, and cardiolipin (CL) of hypertrophied hearts. The associated changes in fatty acyl composition were specific for the individual phospholipid class as evidenced by a significant elevation of palmitic acid in PC, docosahexaenoic acid in PE and oleic acid in CL. Alterations in fatty acyl composition of phospholipids were associated with no change in the composition of cardiac triglycerides, cardiac free fatty acids or serum lipids. The fatty acyl composition of phospholipids was also altered in pressure-overload hypertrophied hearts of cats, as evidenced by a reduction of linoleic acid and an elevation of arachidonic acid in total phospholipids. These findings demonstrate that changes in phospholipid metabolism occur in the pressure-overloaded mammalian heart. Such alterations may contribute to altered membrane function in the hypertrophied myocardium.

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