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J. Bacteriol., Aug 1996, 4794-4800, Vol 178, No. 16
HR Morbidoni, D de Mendoza and JE Cronan Jr
A cluster of Bacillus subtilis fatty acid synthetic genes was isolated by
complementation of an Escherichia coli fabD mutant encoding a
thermosensitive malonyl coenzyme A-acyl carrier protein transacylase. The
B. subtilis genomic segment contains genes that encode three fatty acid
synthetic proteins, malonyl coenzyme A-acyl carrier protein transacylase
(fabD), 3-ketoacyl-acyl carrier protein reductase (fabG), and the
N-terminal 14 amino acid residues of acyl carrier protein (acpP). Also
present is a sequence that encodes a homolog of E. coli plsX, a gene that
plays a poorly understood role in phospholipid synthesis. The B. subtilis
plsX gene weakly complemented an E. coli plsX mutant. The order of genes in
the cluster is plsX fabD fabG acpP, the same order found in E. coli, except
that in E. coli the fabH gene lies between plsX and fabD. The absence of
fabH in the B. subtilis cluster is consistent with the different fatty acid
compositions of the two organisms. The amino acid sequence of B. subtilis
acyl carrier protein was obtained by sequencing the purified protein, and
the sequence obtained strongly resembled that of E. coli acyl carrier
protein, except that most of the protein retained the initiating methionine
residue. The B. subtilis fab cluster was mapped to the 135 to 145 degrees
region of the chromosome.
Copyright © 1996, American Society for Microbiology
Bacillus subtilis acyl carrier protein is encoded in a cluster of lipid biosynthesis genes
Department of Microbiology, University of Illinois, Urbana 61801, USA.
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