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FURTHER MOLECULAR CHARACTERIZATION OF THE CLONED LEGIONELLA-PNEUMOPHILA ZINC METALLOPROTEASE INFECTION AND IMMUNITY Moffat, J. F., BLACK, W. J., Tompkins, L. S. 1994; 62 (2): 751-753

Abstract

On the basis of DNA sequence similarities to other Zn metalloproteases, further studies of the synthesis, processing, and enzymatic structure of the cloned Legionella protease gene, proA, were initiated. TnphoA fusions indicated that the entire proA open reading frame was transcribed and translated, including the 5' leader sequence. The results also suggested that the entire polypeptide was exported to the periplasm before cleavage to produce the mature protease. A site-directed mutation in the putative active site, changing glutamate 378 to asparagine, abolished proteolytic activity and cytotoxicity.

View details for Web of Science ID A1994MR84100062

View details for PubMedID 8300238

View details for PubMedCentralID PMC186173