The Response of Escherichia Coli to Fatty Acid Supplements and the Regulation of Membrane Lipid Synthesis

1971 ◽  
pp. 15-31 ◽  
Author(s):  
Salih J. Wakil ◽  
M. Esfahani
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Lipid Synthesis ◽  
Membrane Lipid

scholarly journals Gene-Specific Random Mutagenesis of Escherichia coli In Vivo: Isolation of Temperature-Sensitive Mutations in the Acyl Carrier Protein of Fatty Acid Synthesis

2006 ◽  
Vol 188 (1) ◽  
pp. 287-296 ◽  
Author(s):  
Nicholas R. De Lay ◽  
John E. Cronan
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Acyl Carrier Protein ◽  
Lipid Synthesis ◽  
Acid Synthesis ◽  
Temperature Sensitive ◽  
Carrier Protein ◽  
Nonpermissive Temperature ◽  
Overlap Extension

ABSTRACT Acyl carrier proteins (ACPs) are very small acidic proteins that play a key role in fatty acid and complex lipid synthesis. Moreover, recent data indicate that the acyl carrier protein of Escherichia coli has a large protein interaction network that extends beyond lipid synthesis. Despite extensive efforts over many years, no temperature-sensitive mutants with mutations in the structural gene (acpP) that encodes ACP have been isolated. We report the isolation of three such mutants by a new approach that utilizes error-prone PCR mutagenesis, overlap extension PCR, and phage λ Red-mediated homologous recombination and that should be generally applicable. These mutants plus other experiments demonstrate that ACP function is essential for the growth of E. coli. Each of the mutants was efficiently modified with the phosphopantetheinyl moiety essential for the function of ACP in lipid synthesis, and thus lack of function at the nonpermissive temperature cannot be attributed to a lack of prosthetic group attachment. All of the mutant proteins were largely stable at the nonpermissive temperature except the A68T/N73D mutant protein. Fatty acid synthesis in strains that carried the D38V or A68T/N73D mutations was inhibited upon a shift to the nonpermissive temperature and in the latter case declined to a small percentage of the rate of the wild-type strain.

scholarly journals ISOLATION AND GENETIC ANALYSIS OF CAULOBACTER MUTANTS DEFECTIVE IN CELL SHAPE AND MEMBRANE LIPID SYNTHESIS

Genetics ◽  
1984 ◽  
Vol 108 (4) ◽  
pp. 809-826
Author(s):  
David A Hodgson ◽  
Penny Shaw ◽  
Lucille Shapiro
Keyword(s):  
Fatty Acid ◽  
Genetic Analysis ◽  
Cell Shape ◽  
Lipid Synthesis ◽  
Membrane Lipid ◽  
Water Soluble ◽  
Complex Media ◽  
Orange Pigment ◽  
Substantial Distance

ABSTRACT In this paper we report the isolation, characterization and genetic analysis of several C. crescentus mutants altered in membrane lipid synthesis. One of these, a fatty acid bradytroph, AE6002, was shown to be due to a mutation in the fatA gene. In addition to the presence of the fatA506 mutation, this strain was found to contain two other mutations, one of which caused the production of a water-soluble brown-orange pigment (pigA) and another which caused formation of helical cells (hclA). Expression of the latter two phenotypes required complex media and both were repressed by glucose. However, the lesions were mapped to loci that are separated by a substantial distance. The hclA and the fatA genes mapped close together, possibly implying that comutation had occurred in AE6002. Data are presented that allow the unambiguous identification of a second Fat gene (fatB) in C. crescentus. The map position of another mutation in membrane lipid biogenesis, the glycerol-3-PO4 auxotroph gpsA505, was also determined. During this study the flaZ gene was fine-mapped and the positions of proC and rif changed from the previously reported location.

The Classical, Yet Controversial, First Enzyme of Lipid Synthesis: Escherichia coli Acetyl-CoA Carboxylase

2021 ◽  
Author(s):  
John E. Cronan
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Fatty Acid Synthesis ◽  
Building Block ◽  
Lipid Synthesis ◽  
Acid Synthesis ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Content Type ◽  
Malonyl Coa

SUMMARY Escherichia coli acetyl-CoA carboxylase (ACC), the enzyme responsible for synthesis of the malonyl-CoA, the building block of fatty acid synthesis, is the paradigm bacterial ACC. Many reports on the structures and stoichiometry of the four subunits comprising the active enzyme as well as on regulation of ACC activity and expression have appeared in the almost 20 years since this subject was last reviewed. This review seeks to update and expand on these reports.

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