TY - JOUR
T1 - Transport of long chain fatty acids in Escherichia coli. Identification of a membrane protein associated with the fadL gene
AU - Ginsburgh, C. L.
AU - Black, P. N.
AU - Nunn, W. D.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1984
Y1 - 1984
N2 - The fadL gene is required for the transport of long chain fatty acids in Escherichia coli (Maloy, S.R., Ginsburgh, C.L., Simons, R.W., and Nunn, W.D. (1981) J. Biol. Chem. 256, 3735-3742). In an effort to define the fadL gene product(s), the membrane proteins of 16 independently isolated fadL mutants and wild type strains were compared by two-dimensional gel electrophoretic analysis. These studies indicated that (i) whenever a fadL mutation was present, a 33,000-dalton inner membrane protein was consistently absent, (ii) genetic restoration of mutant alleles to fadL+ resulted in the reappearance of this 33-kDa protein, and (iii) a reversion event mapping to the fadL gene produced a 33-kDa protein with altered electrophoretic properties. Mutations in the other known fad structural genes do not affect 33-kDa protein synthesis and the expression of the 33-kDa protein is physiologically regulated in a manner similar to the known fad enzymes. Overall, these studies suggest there is a close relationship between the 33-kDa inner membrane protein and the fadL gene which putatively codes for a fatty acid transport component(s).
AB - The fadL gene is required for the transport of long chain fatty acids in Escherichia coli (Maloy, S.R., Ginsburgh, C.L., Simons, R.W., and Nunn, W.D. (1981) J. Biol. Chem. 256, 3735-3742). In an effort to define the fadL gene product(s), the membrane proteins of 16 independently isolated fadL mutants and wild type strains were compared by two-dimensional gel electrophoretic analysis. These studies indicated that (i) whenever a fadL mutation was present, a 33,000-dalton inner membrane protein was consistently absent, (ii) genetic restoration of mutant alleles to fadL+ resulted in the reappearance of this 33-kDa protein, and (iii) a reversion event mapping to the fadL gene produced a 33-kDa protein with altered electrophoretic properties. Mutations in the other known fad structural genes do not affect 33-kDa protein synthesis and the expression of the 33-kDa protein is physiologically regulated in a manner similar to the known fad enzymes. Overall, these studies suggest there is a close relationship between the 33-kDa inner membrane protein and the fadL gene which putatively codes for a fatty acid transport component(s).
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M3 - Article
C2 - 6376508
AN - SCOPUS:0021240017
SN - 0021-9258
VL - 259
SP - 8437
EP - 8443
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 13
ER -