ISOLATION OF AN USTILAGO-MAYDIS GENE ENCODING 3-HYDROXY-5-METHYLGLUTARYL-COENZYME-A REDUCTASE AND EXPRESSION OF A C-TERMINAL-TRUNCATED FORMIN ESCHERICHIA-COLI
R. Croxen et al., ISOLATION OF AN USTILAGO-MAYDIS GENE ENCODING 3-HYDROXY-5-METHYLGLUTARYL-COENZYME-A REDUCTASE AND EXPRESSION OF A C-TERMINAL-TRUNCATED FORMIN ESCHERICHIA-COLI, Microbiology, 140, 1994, pp. 2363-2370
A gene encoding 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reduct
ase was isolated from the maize fungal pathogen Ustilago maydis. This
was accomplished by identifying cDNA and genomic clones that hybridize
d to an internal fragment of the gene, amplified from U. maydis genomi
c DNA by PCR. The nature of the gene was determined by nucleotide sequ
ence analysis, and by comparing the derived amino acid sequence of the
gene with HMG-CoA reductases from yeast, and from other organisms. Th
e hydrophobic nature of the N-terminal region of the deduced protein s
equence abo supported the view that this gene encoded HMG-CoA reductas
e. A C-terminal-truncated fragment of the U. maydis HMG-CoA reductase
gene was shown to be expressed in Escherichia coli in a catalytically
active form. The expressed protein was also shown to be sensitive to a
n inhibitor of mammalian HMG-CoA reductase activity.