Abstract:
:The DNA encoding the zinc metalloprotease of Legionella pneumophila Philadelphia 1 has been isolated and expressed in Escherichia coli. This protein, which is 38,000 Daltons in size, possesses immunological and biochemical properties identical to those previously described for the purified L. pneumophila protease. Periplasmic extracts of E. coli clones expressing the recombinant protease are also capable of causing the haemolysis of canine erythrocytes and the cytotoxic destruction of CHO cells. Using transposon mutagenesis, it was determined that a maximum of 1.2 kb of DNA encoded all three biological activities. Inactivation of proteolytic activity by transposon insertion occurred concomitantly with losses of the haemolytic and cytotoxic phenotypes. A putative regulatory sequence approximately 200-500 bp upstream of the gene's coding region was identified. A 4.0 kb fragment encoding these activities hybridized to the chromosomal DNA of the parent strain of L. pneumophila Philadelphia 1 as well as clinical isolates of L. pneumophila.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Quinn FD,Tompkins LSdoi
10.1111/j.1365-2958.1989.tb00228.xsubject
Has Abstractpub_date
1989-06-01 00:00:00pages
797-805issue
6eissn
0950-382Xissn
1365-2958journal_volume
3pub_type
杂志文章abstract::Regulation of polar development and cell division in Caulobacter crescentus relies on the dynamic localization of several proteins to cell poles at specific stages of the cell cycle. The polar organelle development protein, PodJ, is required for the synthesis of the adhesive holdfast and pili. Here we show the cell cy...
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journal_title:Molecular microbiology
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journal_title:Molecular microbiology
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pub_type: 杂志文章
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更新日期:1992-04-01 00:00:00
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