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J. Biol. Chem., Vol. 266, Issue 13, 8551-8559, May, 1991
M Becker-Andre, P Schulze-Lefert and K Hahlbrock
4-Coumarate:CoA ligase (4CL), a key enzyme of phenylpropanoid metabolism in
plants, is encoded in potato (Solanum tuberosum L.) by two structurally
similar genes (St4cl-1, St4cl-2). Computer-based sequence analyses revealed
similarities at the amino acid sequence level with other enzymes dependent
on ATP for activation of aromatic carboxylic acids, e.g. some bacterial
peptide synthetases. All these enzymes have a common seven amino acid
sequence motif containing one cysteine residue. Using an assay on the basis
of the polymerase chain reaction, we show that the mRNAs from both 4CL
genes accumulate to equal levels in suspension-cultured cells and whole
plant tissues, independent of various kinds of activating stimulus applied
and of the overall transcriptional activity of the genes. The apparent lack
of differential expression, together with the fact that both 4CL genes and
proteins are nearly identical in structure, make it unlikely that 4CL
isoforms in potato have specific roles in metabolic channeling.
Constitutive in vivo footprints in the TATA-box proximal region of the
St4cl-1 promoter define putative cis-acting elements which may be involved
in the responses of the 4CL genes to various endogenous and exogenous
stimuli.
Structural comparison, modes of expression, and putative cis-acting elements of the two 4-coumarate: CoA ligase genes in potato
Max-Planck-Institut fur Zuchtungsforschung, Abteilung Biochemie, Koln, Federal Republic of Germany.
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