Abstract
The outer membrane protein FadL (product of the fadL gene) of Escherichia coli is required for the specific binding and transport of exogenous long-chain fatty acids prior to metabolic utilization. The carboxyl end of FadL has been proposed to play a crucial role by facilitating the transport of long-chain fatty acids. In an attempt to define specific amino acid residues within carboxyl region of FadL essential for activity, a series of deletion and point mutations within the 3' end of the fadL+ gene have been constructed and characterized. These fadL mutants were classified into three categories based on functional properties attributable to the altered FadL proteins: (i) those that had essentially wild-type levels of long-chain fatty acid binding and transport, (ii) those that had wild-type levels of long-chain fatty acid binding but were defective in transport, and (iii) those that were defective for both long-chain fatty acid binding and transport. These findings demonstrate that amino acid residues Phe448, Pro428, Val410, and Ser397 are required for optimal levels of long-chain fatty acid transport and that amino acid residues Pro428 and Val410 are essential for long-chain fatty acid binding.
Highlights
The outer membrane protein FadL of Escherichia coli is required for the spe- across the inner membrane prior tometabolic utilization [3]
The carboxyl acids across the periplasmic space and the inner membrane end of FadL has been proposed to play a crucial role have not been defined
In an attempt to define specific amino acid residues within carboxyl region of FadL essential for activity, a series of deletion and point mutations within the 3’ end of the fadL+gene have been constructed and characterized. These fadL mutants wereclassifiedinto three categoriesbased on functional properties attributable to the altered FadL proteins: (i) those that had essentiallywild-typelevels of long-chain fatty acid binding and transport, (ii) those that had wild-type levels of long-chain fatty acid binding but were defective in transport, and (iii)those that were defectivefor both long-chain fatty acid binding and transport. These findings demonstrate that amino acid residues Phe44s, acid (CI8:.)-binding protein that hasbeen postulated tobe an H+/fatty acid cotransporter in the inner membran(e9, 10)
Summary
Prototrophic fadR fadR::TnlO )adR AfadL5 fadR zea::TnlO fadD fadR AfadL5 zea::TnlOfadD88 thi thrl leu lacy tonA22. OmpF62 AfadL701 relA pit spoTl T2RAfadR Hfr P02A tonA22 AphoA8 ompF627, AfadL701 relA pit spoTl T2RAfadR srlA::TnlO recA Hfr P02A tonA22 AphoA8 ompF627 AfadL701 relA pit spoTl T2RfadR::TnlO Hfr P02A tonA22 AphoA8 ompF627 AfadL701 relA pit spoTl T2R thi supE A(lac-proAB) mutS::TnlO [FproA+B+ laqZq ZAM151 endAl recAl gyrA96 thi hsdR17 (rk-, mk-) relAl supE44 X- A (lac-proAB) [F' traD36proAB hqZq ZAM151 thi thr' leu lacy tonA22 supE44 AtrpE
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