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Bacterial aspartic proteinases
Author(s) -
Hill Jeffrey,
Phylip Lowri H
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00547-4
Subject(s) - pepstatin , recombinant dna , escherichia coli , biochemistry , aspartic acid , biology , genomic dna , bacteria , dna , enzyme , microbiology and biotechnology , chemistry , amino acid , gene , protease , genetics
Regions of genomic DNA encoding putative aspartic proteinase domains were amplified by PCR from the bacterial species, Escherichia coli and Haemophilus influenzae . Expression of each of these DNA fragments resulted in the accumulation of the corresponding recombinant proteins in insoluble aggregates. Each recombinant protein was solubilised, refolded and shown to be able to cleave synthetic peptides that have been extensively used previously as substrates for aspartic proteinases of vertebrate, fungal and retroviral origin. Each activity was completely blocked by the diagnostic aspartic proteinase inhibitor, acetyl‐pepstatin. This is thus the first report demonstrating unequivocally that aspartic proteinases may be present in bacteria.