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Microbiology 142 (1996), 2969-2974; DOI  10.1099/13500872-142-10-2969
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The thij locus and its relation to phosphorylation of hydroxymethylpyrimidine in Escherichia coli

Tomoko Mizote1, Masataka Tsuda2, Teruko Nakazawa2 and Hideo Nakayama1,3,{dagger}

1Department of Food and Nutrition, Yamaguchi Prefectural University, 3-2-1 Sakurabatake, Yamaguchi 753, Japan
2Department of Microbiology, Yamaguchi University School of Medicine, Ube, Yamaguchi 755, Japan

3Author for correspondence: Hideo Nakayama. Tel: +81 836 58 5360. Fax: +81 836 58 5362.

ABSTRACT

Extracts from Escherichia coli K-12 contained two distinct enzymes capable of catalysing the phosphorylation of hydroxymethylpyrimidine (HMP) to HMP monophosphate: pyridoxine kinase (EC 2.7.1.35) and an enzyme that has not previously been genetically analysed, HMP kinase (EC 2.7.1.49). Two distinct genes, pdxL and thiJ, specify the activities of the former and latter enzymes, respectively. The inactivation of both genes by independent mutations in the same cell resulted in the complete loss of HMP kinase activity. Experiments with a series of strains that carry mutations in thiC, thiC pdxB, thiC pdxB pdxL and thiC pdxB pdxL thiJ revealed that the ability of the double mutant (pdxL thiJ) to utilize HMP in thiamin pyrophosphate biosynthesis was restored by introducing the wild-type allele corresponding to the thiJ mutation. The thiJ locus was mapped on the chromosome near the thiD and thiM loci, which govern the activities of phosphomethylpyrimidine kinase (EC 2.7.4.7) and hydroxyethylthiazole kinase (EC 2.7.1.50), respectively.

Keywords: Escherichia coli, thiamin biosynthesis, thiJ locus, hydroxymethylpyrimidine

{dagger} Present address: Department of Internal Medicine, Sea-Side Hospital, Maruo, Higashikiwa, Ube 755-02, Japan.




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