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J. Biol. Chem., Vol. 263, Issue 5, 2146-2151, 02, 1988
JA Rafalski and SC Falco
The yeast HOM3 gene has been cloned molecularly by complementation of a
HOM3 mutant. The gene is located about 8 kilobase pairs from HIS1 and is
present as a single copy in the yeast genome. Mutations in HOM3 result in a
requirement for threonine and methionine (or homoserine) for growth and a
lack of detectable aspartokinase activity. The nucleotide sequence of HOM3
predicts an enzyme 414 amino acids long that shows homology to the three
Escherichia coli aspartokinases, indicating that it is the structural gene
for yeast aspartokinase. An approximately 1800-base pair mRNA is
transcribed from the HOM3 gene, initiating at several start sites, 80 and
70 base pairs downstream, respectively, from two TATA boxes. Upstream of
the TATA boxes is a single TGACTC sequence. This sequence has been shown to
be essential for regulation of several genes that encode amino acid
biosynthetic enzymes by the general control system. However, no increase in
aspartokinase mRNA is observed under general control derepressing
conditions.
Structure of the yeast HOM3 gene which encodes aspartokinase [published erratum appears in J Biol Chem 1990 Sep 5;265(25):15346]
Du Pont Experimental Station, Central Research and Development Department, Wilmington, Delaware 19898.
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