Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis. Academic Article

abstract

• The characterization of a three-gene operon (the thiC operon) at 331 min, which is involved in thiamine biosynthesis in Bacillus subtilis, is described. The first gene in the operon is homologous to transcription activators in the lysR family. The second and third genes (thiK and thiC) have been subcloned and overexpressed in Escherichia coli. ThiK (30 kDa) catalyzes the phosphorylation of 4-methyl-5-(beta-hydroxyethyl)thiazole. ThiC (27 kDa) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate by 4-methyl-5-(beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. Transcription of the thiC operon is not regulated by thiamine or 2-methyl-4-amino-5-hydroxymethylpyrimidine and is only slightly repressed by 4-methyl-5-(beta-hydroxyethyl)thiazole.

authors

• Begley, Tadhg

published proceedings

• J Bacteriol

altmetric score

• 3

author list (cited authors)

• Zhang, Y., Taylor, S. V., Chiu, H. J., & Begley, T. P.

citation count

• 47

complete list of authors

• Zhang, Y||Taylor, SV||Chiu, HJ||Begley, TP

publication date

• May 1997

publisher

• American Society for Microbiology  Publisher

published in

• Journal of Bacteriology  Journal

keywords

• Amino Acid Sequence
• Bacillus Subtilis
• Bacterial Proteins
• Base Sequence
• Cloning, Molecular
• DNA Primers
• Escherichia Coli
• Gene Expression Regulation, Bacterial
• Molecular Sequence Data
• Operon
• Recombinant Proteins
• Sequence Homology, Amino Acid
• Thiamine
• Trans-Activators
• Transcription, Genetic

PubMed Central ID

• 9139923

Digital Object Identifier (DOI)

• 10.1128/jb.179.9.3030-3035.1997

start page

• 3030

end page

• 3035

volume

• 179

issue

• 9

URL

• http%3A%2F%2Fdx.doi.org%2F10.1128%2Fjb.179.9.3030-3035.1997