title: Molecular cloning and sequence analysis of the proC gene encoding delta 1-pyrroline-5-carboxylate reductase from an extremely thermophilic eubacterium Thermus thermophilus.
abstract: A gene library of the extremely thermophilic bacterium, Thermus thermophilus HB27, was constructed in Escherichia coli, and recombinant plasmids able to complement proC mutants of HB27 were obtained. Using the plasmids, the complete nucleotide sequence of the proC gene encoding delta 1-pyrroline-5-carboxylate reductase (P5CR) [EC 1.5.1.2] was determined. The deduced amino acid sequence showed a significant homology to those of P5CRs of E. coli, soybean and human. The proC gene of T. thermophilus was expressed in E. coli and the activity of heat-resistant P5CR was determined. The mutation sites of two HB27 proC mutants were also determined.
authors.affiliation: Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Hoshino
authors.forename: T
authors.initials: T
authors.lastname: Kosuge
authors.forename: Y
authors.initials: Y
authors.lastname: Hidaka
authors.forename: K
authors.initials: K
authors.lastname: Tabata
authors.forename: T
authors.initials: T
authors.lastname: Nakahara
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003062:Codon; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D017354:Point Mutation; D011762:Pyrroline Carboxylate Reductases / Q000235:genetics*; D015183:Restriction Mapping; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D016963:Thermus thermophilus / Q000201:enzymology*
chemical_list: D003062:Codon; D011762:Pyrroline Carboxylate Reductases