Phase transitions of phospholipid bilayers from an unsaturated fatty acid auxotroph of Escherichia coli

1977 ◽  
Vol 466 (3) ◽  
pp. 393-401 ◽  
Author(s):  
Kaku Uehara ◽  
Hideo Akutsu ◽  
Yoshimasa Kyogoku ◽  
Yuzuru Akamatsu
Keyword(s):  
Escherichia Coli ◽  
Phase Transitions ◽  
Fatty Acid ◽  
Unsaturated Fatty Acid ◽  
Phospholipid Bilayers ◽  
Fatty Acid Auxotroph

scholarly journals Turnover of Phospholipids in an Unsaturated Fatty Acid Auxotroph of Escherichia coli

1972 ◽  
Vol 112 (3) ◽  
pp. 1396-1407 ◽  
Author(s):  
Peter D. Crowfoot ◽  
Tetsuo Oka ◽  
Mojtaba Esfahani ◽  
Salih J. Wakil
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Unsaturated Fatty Acid ◽  
Fatty Acid Auxotroph

Phosphatidylethanolamine molecular species of fatty acid auxotroph of Escherichia coli grown with elaidate

1975 ◽  
Vol 409 (2) ◽  
pp. 212-217 ◽  
Author(s):  
Nishihara Masateru ◽  
Kimura Kazuko ◽  
Izui Katsura ◽  
Ishinaga Masataka ◽  
Kato Michie ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Molecular Species ◽  
Fatty Acid Auxotroph

scholarly journals Escherichia coli FadR Positively Regulates Transcription of the fabB Fatty Acid Biosynthetic Gene

2001 ◽  
Vol 183 (20) ◽  
pp. 5982-5990 ◽  
Author(s):  
John W. Campbell ◽  
John E. Cronan
Keyword(s):  
Escherichia Coli ◽  
Fatty Acid ◽  
Unsaturated Fatty Acid ◽  
Protein A ◽  
Transcriptional Level ◽  
Biosynthetic Gene ◽  
Biochemical Tests ◽  
Mobility Shift ◽  
Mobility Shift Assay ◽  
Gel Mobility Shift

ABSTRACT In Escherichia coli expression of the genes of fatty acid degradation (fad) is negatively regulated at the transcriptional level by FadR protein. In contrast the unsaturated fatty acid biosynthetic gene, fabA, is positively regulated by FadR. We report that fabB, a second unsaturated fatty acid biosynthetic gene, is also positively regulated by FadR. Genomic array studies that compared global transcriptional differences between wild-type and fadR-null mutant strains, as well as in cultures of each strain grown in the presence of exogenous oleic acid, indicated that expression of fabBwas regulated in a manner very similar to that of fabAexpression. A series of genetic and biochemical tests confirmed these observations. Strains containing both fabB andfadR mutant alleles were constructed and shown to exhibit synthetic lethal phenotypes, similar to those observed infabA fadR mutants. A fadR strain was hypersensitive to cerulenin, an antibiotic that at low concentrations specifically targets the FabB protein. A transcriptional fusion of chloramphenicol acetyltransferase (CAT) to the fabBpromoter produces lower levels of CAT protein in a strain lacking functional FadR. The ability of a putative FadR binding site within thefabB promoter to form a complex with purified FadR protein was determined by a gel mobility shift assay. These experiments demonstrate that expression of fabB is positively regulated by FadR.

Lipid profiles of conidia of Aspergillus niger and a fatty acid auxotroph

1987 ◽  
Vol 33 (12) ◽  
pp. 1116-1120 ◽  
Author(s):  
Panchanon Chattopadhyay ◽  
Santu Kumar Banerjee ◽  
Kalyani Sen ◽  
Parul Chakrabarti
Keyword(s):  
Fatty Acids ◽  
Fatty Acid ◽  
Double Bond ◽  
Aspergillus Niger ◽  
Fatty Acid Profile ◽  
Unsaturated Fatty Acid ◽  
Desaturase Activity ◽  
Wild Type ◽  
Type V ◽  
Fatty Acid Auxotroph

Conidial lipids of the wild-type (V35) Aspergillus niger and its unsaturated fatty acid auxotroph (UFA2) were compared. The wild type contained lower levels (7.6%) of phospholipids and higher levels (28.4%) of glycolipids than the mutant (16.5 and 22.2%, respectively). Oleic (33.4%), linoleic (22.5%), palmitic (12.8%), stearic (7.4%), and linolenic (6.2%) were the main fatty acids of the wild type (V35). The mutant grew only in the presence of unsaturated fatty acid having at least one Δ9cis double bond, and its conidial fatty acid profile was influenced by the exogenous acid. Analyses of the fatty acids of UFA2 grown in the presence of different fatty acid supplements support the original view that the mutant is defective in Δ9-desaturase activity.

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