This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hove-Jensen, B Search for Related Content PubMed PubMed Citation Articles by Hove-Jensen, B

research-article

Identification of tms-26 as an allele of the gcaD gene, which encodes N-acetylglucosamine 1-phosphate uridyltransferase in Bacillus subtilis.

University Institute of Biological Chemistry B, Copenhagen, Denmark.

ABSTRACT

The temperature-sensitive Bacillus subtilis tms-26 mutant strain was characterized biochemically and shown to be defective in N-acetylglucosamine 1-phosphate uridyltransferase activity. At the permissive temperature (34 degrees C), the mutant strain contained about 15% of the wild-type activity of this enzyme, whereas at the nonpermissive temperature (48 degrees C), the mutant enzyme was barely detectable. Furthermore, the N-acetylglucosamine 1-phosphate uridyltransferase activity of the tms-26 mutant strain was much more heat labile in vitro than that of the wild-type strain. The level of N-acetylglucosamine 1-phosphate, the substrate of the uridyltransferase activity, was elevated more than 40-fold in the mutant strain at the permissive temperature compared with the level in the wild-type strain. During a temperature shift, the level of UDP-N-acetylglucosamine, the product of the uridyltransferase activity, decreased much more in the mutant strain than in the wild-type strain. An Escherichia coli strain harboring the wild-type version of the tms-26 allele on a plasmid contained increased N-acetylglucosamine 1-phosphate uridyltransferase activity compared with that in the haploid strain. It is suggested that the gene for N-acetylglucosamine 1-phosphate uridyltransferase in B. subtilis be designated gcaD.

This article has been cited by other articles:

• Hove-Jensen, B. (2004). Heterooligomeric Phosphoribosyl Diphosphate Synthase of Saccharomyces cerevisiae: COMBINATORIAL EXPRESSION OF THE FIVE PRS GENES IN ESCHERICHIA COLI. J. Biol. Chem. 279: 40345-40350 [Abstract] [Full Text]  
• Hove-Jensen, B., Rosenkrantz, T. J., Haldimann, A., Wanner, B. L. (2003). Escherichia coli phnN, Encoding Ribose 1,5-Bisphosphokinase Activity (Phosphoribosyl Diphosphate Forming): Dual Role in Phosphonate Degradation and NAD Biosynthesis Pathways. J. Bacteriol. 185: 2793-2801 [Abstract] [Full Text]  
• Krath, B. N., Hove-Jensen, B. (2001). Implications of secondary structure prediction and amino acid sequence comparison of class I and class II phosphoribosyl diphosphate synthases on catalysis, regulation, and quaternary structure. Protein Sci. 10: 2317-2324 [Abstract] [Full Text]  
• Bulik, D. A., van Ophem, P., Manning, J. M., Shen, Z., Newburg, D. S., Jarroll, E. L. (2000). UDP-N-acetylglucosamine Pyrophosphorylase, a Key Enzyme in Encysting Giardia, Is Allosterically Regulated. J. Biol. Chem. 275: 14722-14728 [Abstract] [Full Text]  
• Hernando, Y., Carter, A. T., Parr, A., Hove-Jensen, B., Schweizer, M. (1999). Genetic Analysis and Enzyme Activity Suggest the Existence of More Than One Minimal Functional Unit Capable of Synthesizing Phosphoribosyl Pyrophosphate in Saccharomyces cerevisiae. J. Biol. Chem. 274: 12480-12487 [Abstract] [Full Text]  
• Krath, B. N., Hove-Jensen, B. (1999). Organellar and Cytosolic Localization of Four Phosphoribosyl Diphosphate Synthase Isozymes in Spinach. Plant Physiol. 119: 497-506 [Abstract] [Full Text]  
• Pompeo, F., van Heijenoort, J., Mengin-Lecreulx, D. (1998). Probing the Role of Cysteine Residues in Glucosamine-1-Phosphate Acetyltransferase Activity of the Bifunctional GlmU Protein from Escherichia coli: Site-Directed Mutagenesis and Characterization of the Mutant Enzymes. J. Bacteriol. 180: 4799-4803 [Abstract] [Full Text]  
• Pompeo, F., Bourne, Y., van Heijenoort, J., Fassy, F., Mengin-Lecreulx, D. (2001). Dissection of the Bifunctional Escherichia coli N-Acetylglucosamine-1-phosphate Uridyltransferase Enzyme into Autonomously Functional Domains and Evidence That Trimerization Is Absolutely Required for Glucosamine-1-phosphate Acetyltransferase Activity and Cell Growth. J. Biol. Chem. 276: 3833-3839 [Abstract] [Full Text]  
• Krath, B. N., Hove-Jensen, B. (2001). Class II Recombinant Phosphoribosyl Diphosphate Synthase from Spinach. PHOSPHATE INDEPENDENCE AND DIPHOSPHORYL DONOR SPECIFICITY. J. Biol. Chem. 276: 17851-17856 [Abstract] [Full Text]