PMID:3549687
| Citation |
Jackowski, S and Rock, CO (1987) Altered molecular form of acyl carrier protein associated with beta-ketoacyl-acyl carrier protein synthase II (fabF) mutants. J. Bacteriol. 169:1469-73 |
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| Abstract |
Acyl carrier protein (ACP) is a required cofactor for fatty acid synthesis in Escherichia coli. Mutants lacking beta-ketoacyl-ACP synthase II activity (fabF1 or fabF3) possessed a different molecular species of ACP (F-ACP) that was separated from the normal form of the protein by conformationally sensitive gel electrophoresis. Synthase I mutants contained the normal protein. Complementation of fabF1 mutants with an F' factor harboring the wild-type synthase II allele resulted in the appearance of normal ACP, whereas complementation with an F' possessing the fabF2 allele (a mutation that produces a synthase II enzyme with altered catalytic activity) resulted in the production of both forms of ACP. The structural difference between F-ACP and ACP persisted after the removal of the 4'-phosphopantetheine prosthetic group, and both forms of the protein had identical properties in an in vitro fatty acid synthase assay. Both ACP and F-ACP were purified to homogeneity, and their primary amino acid sequences were determined. The two ACP species were identical but differed from the sequence reported for E. coli E-15 ACP in that an Asn instead of an Asp was at position 24 and an Ile instead of a Val was at position 43. Therefore, F-ACP appears to be a modification of ACP that is detected when beta-ketoacyl-ACP synthase II activity is impaired. |
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| Keywords |
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/genetics; 3-Oxoacyl-(Acyl-Carrier-Protein) Synthase/metabolism; Acyl Carrier Protein/analysis; Acyl Carrier Protein/isolation & purification; Acyl Carrier Protein/metabolism; Acyltransferases/genetics; Amino Acid Sequence; Escherichia coli/analysis; Escherichia coli/enzymology; Escherichia coli/genetics; Fatty Acids/biosynthesis; Genetic Complementation Test; Mutation; Oleic Acids/biosynthesis |
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