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

Author:

Black P N1

Affiliation:

1. Department of Biochemistry, College of Medicine, University of Tennessee, Memphis 38163.

Abstract

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference38 articles.

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3. Cytodifferentiation in the accessory glands of Tenebrio molitor. VII. Crossed immunoelectrophoretic analysis of terminal differentiation in the post-ecdysial tubular accessory glands;Black P. N.;Dev. Biol.,1982

4. Purification and characterization of an outer membrane-bound protein involved in long-chain fatty acid transport in Escherichia coli;Black P. N.;J. Biol. Chem.,1987

5. Receptor for bacteriophage lambda of Escherichia coli forms larger pores in black lipid membranes than the matrix protein (porin);Boehler-Kohler B. A.;J. Bacteriol.,1979

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