Effects of dam and/or seqA mutations on the fatty acid and phospholipid membrane composition of Salmonella enterica serovar Typhimurium.
We examined the phospholipids (Phls) and the membrane fatty acid (FA) composition in Salmonella enterica serovar Typhimurium dam and/or seqA mutants. Phosphatidylglycerol, phosphatidylethanolamine (PE), and cardiolipin (CL) are the major Phls present in all the strains and accounted for greater than 95% of the total lipid phosphorus. Phosphatidic acid and phosphatidylserine are the minor ones. The seqA mutant showed a decrease in PE and an increase in CL and phosphatidylglycerol proportion compared with the wild-type strain. The same changes were observed with the seqA dam double mutant. However, the dam mutation caused an unusual accumulation of CL with a significant decrease in the PE content, compared with the isogenic wild-type strain. FA composition of the total lipids and the different fractions containing Phls have been determined. The major saturated FAs (SFAs) and unsaturated FAs (UFAs) found were C(14:0), C(16:0) and C(16:1w7), C(18:1w9), respectively. Cyclic FAs, cyc(17:0) and cyc(19:0), were also present in appreciable amounts. Moreover, dam and/or seqA mutations caused a decrease in UFA/SFA ratio and there was a progressive reduction in the content of C(16:1w7) and C(18:1w9), going through the order seqA, dam/seqA, and dam mutants. This decrease in UFA content was compensated for in all strains by an increase in the corresponding C(17-) and C(19-) cyclic FAs. So these UFAs were converted to their cyclopropane derivatives, which resulted in a low UFA/SFA ratio. SeqA and Dam proteins might regulate FA biosynthesis and Phls composition of Salmonella enterica serovar Typhimurium.
Laboratory of Biochemistry and Molecular Biology, Faculty of Sciences of Bizerte, Zarzouna, Tunisia. aminealoui@yahoo.fr
Amine
A
Aloui
Mouadh
M
Mihoub
Mohamed Marwan
MM
Sethom
Abdelwaheb
A
Chatti
Moncef
M
Feki
Naziha
N
Kaabachi
Ahmed
A
Landoulsi
D000146:Acids, Carbocyclic / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics* / Q000502:physiology; D002308:Cardiolipins / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000235:genetics* / Q000502:physiology; D005227:Fatty Acids / Q000378:metabolism*; D008563:Membrane Lipids / Q000378:metabolism*; D009154:Mutation; D010714:Phosphatidylethanolamines / Q000378:metabolism; D010715:Phosphatidylglycerols / Q000378:metabolism; D010743:Phospholipids / Q000378:metabolism; D018741:Replication Origin; D012486:Salmonella typhimurium / Q000235:genetics* / Q000378:metabolism* / Q000472:pathogenicity; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific) / Q000235:genetics* / Q000502:physiology; D014774:Virulence
D000146:Acids, Carbocyclic; D001425:Bacterial Outer Membrane Proteins; D002308:Cardiolipins; D004268:DNA-Binding Proteins; D005227:Fatty Acids; D008563:Membrane Lipids; D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; D010743:Phospholipids; C058693:Dam methyltransferase; D015265:Site-Specific DNA-Methyltransferase (Adenine-Specific)