Further molecular characterization of the cloned Legionella pneumophila zinc metalloprotease.
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.
Moffat
J F
JF
Department of Microbiology and Immunology, Stanford University Medical School, California.
Black
W J
WJ
Tompkins
L S
LS
D000818:Animals; D001426:Bacterial Proteins; D001665:Binding Sites / Q000235:genetics; D016923:Cell Death / Q000187:drug effects; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D006801:Humans; D066298:In Vitro Techniques; D016952:Legionella pneumophila / Q000201:enzymology* / Q000235:genetics*; D008666:Metalloendopeptidases / Q000235:genetics* / Q000378:metabolism / Q000633:toxicity; D016297:Mutagenesis, Site-Directed; D016366:Open Reading Frames; D017354:Point Mutation; D011499:Protein Processing, Post-Translational
D001426:Bacterial Proteins; D008666:Metalloendopeptidases; C043859:pseudolysin, Pseudomonas aeruginosa