Kong D, Husson RN; American Society for Microbiology. General Meeting.
Abstr Gen Meet Am Soc Microbiol. 1997 May 4-8; 97: 563 (abstract no. U114).
Childrens Hospital, Boston, MA.
D-Fructose 1,6-bisphosphate (FBP) aldolases are key glycolytic pathway enzymes, which catalyze the reversible aldol cleavage of Fructose-bisphophate into glyceradehyde 3-phosphate and dihydroxyacetone phosphate. FBP aldolases have been divided into two classes (class I and class II) based on their catalytic and structural properties. Both of class I and class II aldolases have been reported to exist in M. tuberculosis, and their expression was regulated by oxygen tension. Class I aldolases were dominantly expressed under conditions of high oxygen tension, while class II aldolase expression was increased at low oxygen tension. In addition, it has been reported that non-pathogenic M. smegmatis possess only a class I type aldolase. To investigate the regulation of aldolase in mycobacteria and the possible role that the aldolases play in the pathogenesis of M. tuberculosis, we cloned the class II aldolase gene from M. tuberculosis H37Rv by PCR and then by screening a lambda gt11 library using the PCR probe. Sequence analysis demonstrated that this gene encodes a protein of 344 amino acids, which is 74% identical to the class II aldolase gene of Corynebacterium glutamicum. Two promoters were identified in the 5 region of the class II aldolase gene of TB by primer extension and analysis of promoter activity using beta-galactosidase as a reporter gene. In addition, we found that a class II aldolase gene is present in M. smegmatis by Southern blotting and by cloning the gene using the TB class II aldolase gene as a probe. The regulation of class II aldolase gene expression by oxygen tension and its possible role in the pathogenesis of TB are under investigation.
Publication Types:
Keywords:
- Cloning, Organism
- Fructose-Bisphosphate Aldolase
- Gene Expression
- Polymerase Chain Reaction
- Promoter Regions (Genetics)
- Sequence Analysis
- genetics
Other ID:
UI: 102235513
From Meeting Abstracts