title: Sequence and characterization of mutT from Proteus vulgaris.
abstract: A cloned DNA fragment containing the tryptophanase (tna) operon of Proteus vulgaris was found to contain a gene analogous to mutT of Escherichia coli immediately distal to the tna operon. The presumptive mutT of P. vulgaris was shown to be a functional gene by complementation of a mutT mutant from E. coli. The deduced amino acid sequence of the MutT polypeptide of P. vulgaris was 47% identical and 70% similar to MutT of E. coli. The mutT and tna operons of P. vulgaris were shown to be adjacent on the genome of this organism. These operons are located about 20 min apart in the E. coli genome. Our findings suggest that either or both tna and mutT have different genomic locations in the two organisms.
authors.affiliation: Department of Biological Sciences, Stanford University, CA 94305-5020.
authors.forename: A V
authors.initials: AV
authors.lastname: Kamath
authors.forename: C
authors.initials: C
authors.lastname: Yanofsky
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics*; D001483:Base Sequence; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D029968:Escherichia coli Proteins; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D009876:Operon; D010744:Phosphoric Monoester Hydrolases; D011514:Proteus vulgaris / Q000235:genetics*; D011755:Pyrophosphatases; D017386:Sequence Homology, Amino Acid; D014368:Tryptophanase / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D010744:Phosphoric Monoester Hydrolases; D011755:Pyrophosphatases; C052211:mutT protein, E coli; D014368:Tryptophanase