Open AccessMolecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene
Author(s) -
Maximillian T. Follettie,
Anthony J. Sinskey
Publication year - 1986
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.167.2.695-702.1986
Subject(s) - corynebacterium glutamicum , biology , chorismate mutase , nucleic acid sequence , corynebacterium , biochemistry , molecular cloning , gene , dehydratase , structural gene , escherichia coli , gene product , microbiology and biotechnology , peptide sequence , genetics , gene expression , biosynthesis , bacteria
The pheA gene of Corynebacterium glutamicum encoding prephenate dehydratase was isolated from a gene bank constructed in C. glutamicum. The specific activity of prephenate dehydratase was increased six-fold in strains harboring the cloned gene. Genetic and structural evidence is presented which indicates that prephenate dehydratase and chorismate mutase were catalyzed by separate enzymes in this species. The C. glutamicum pheA gene, subcloned in both orientations with respect to the Escherichia coli vector pUC8, was able to complement an E. coli pheA auxotroph. The nucleotide sequence of the C. glutamicum pheA gene predicts a 315-residue protein product with a molecular weight of 33,740. The deduced protein product demonstrated sequence homology to the C-terminal two-thirds of the bifunctional E. coli enzyme chorismate mutase-P-prephenate dehydratase.