Cloning and expression of the aspartate carbamoyltransferase gene from Treponema denticola

Article Abstract:

An investigation was conducted to clone and characterize antigenic proteins of Treponema denticola, an oral spirochete associated with the subgingival plaque in periodontitis. One clone chosen for further analysis coded for a protein with 33.8% homology to the aspartate carbamoyltransferase (ATCase) of Escherichia coli. The protein-coding region was isolated and expressed in E. coli, and the expressed product was partially purified. Enzyme assays on the partially purified product revealed the presence of ATCase activity. Furthermore, the protein reacted with antisera against T. denticola, demonstrating its antigenicity.

Transferases, Periodontal disease, Periodontal diseases

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Activation of plasma membrane H+-ATPase and expression of PMA1 and PMA2 genes in Saccharomyces cerevisiae cells grown at supraoptimal temperatures

Article Abstract:

When Saccharomyces cerevisiae cells are exposed to temperatures higher than their optimal growing temperature the ATPase activity of the plasma membrane and activity of the gene PMA2 increases, but the activity of the gene PMA1 and the amount of ATPase protein in the membrane decreases. The genes PMA1 and PMA2 are responsible for the plasma membrane's H+-ATPase activity and normally PMA2 is less active than PMA1. The increased ATPase activity is due to either a change in the PMA1 ATPase after it is formed or a change in the fluidity of the plasma membrane.

Adenosine triphosphatase genes, ATP genes

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Induction by alpha-L-arabinose and alpha-L-rhamnose of endopolygalacturonase gene expression in Colletotrichum lindemuthianum

Article Abstract:

The fungal pathogen Colletotrichum lindemuthianum increased its production of endopolygalacturonase (endoPG) when it was grown in liquid medium with L-arabinose or L-rhamnose as the only source of carbon. The endolytic nature of the enzyme was shown through its specific interaction with the polygalacturonase-inhibiting protein of the host plant as well as by sugar analysis of the products released from its action on oligogalacturonides.

Microbial enzymes, Bacteria, Phytopathogenic, Phytopathogenic bacteria

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