The fadL gene product of Escherichia coli is an outer membrane protein required for uptake of long-chain fatty acids and involved in sensitivity to bacteriophage T2.
The fadL+ gene of Escherichia coli encodes an outer membrane protein (FadL) essential for the uptake of long-chain fatty acids (C12 to C18). The present study shows that in addition to being required for uptake of and growth on the long-chain fatty acid oleate (C18:1), FadL acts as a receptor of bacteriophage T2. Bacteriophage T2-resistant (T2r) strains lacked FadL and were unable to take up and grow on long-chain fatty acids. Upon transformation with the fadL+ clone pN103, T2r strains became sensitive to bacteriophage T2 (T2s), became able to take up long-chain fatty acids at wild-type levels, and contained FadL in the outer membrane.
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Department of Biochemistry, College of Medicine, University of Tennessee, Memphis 38163.
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins; D050612:Fatty Acid Transport Proteins; D005227:Fatty Acids / Q000378:metabolism*; D007163:Immunosorbent Techniques; D019301:Oleic Acid; D009829:Oleic Acids / Q000378:metabolism; D013604:T-Phages / Q000472:pathogenicity*
D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D050612:Fatty Acid Transport Proteins; D005227:Fatty Acids; D009829:Oleic Acids; C065691:fadL protein, E coli; D019301:Oleic Acid