BACTERIAL ASPARTIC PROTEINASES

Authors
Citation
J. Hill et Lh. Phylip, BACTERIAL ASPARTIC PROTEINASES, FEBS letters, 409(3), 1997, pp. 357-360
Citations number
27
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
409
Issue
3
Year of publication
1997
Pages
357 - 360
Database
ISI
SICI code
0014-5793(1997)409:3<357:BAP>2.0.ZU;2-V
Abstract
Regions of genomic DNA encoding putative aspartic proteinase domains w ere amplified by PCR from the bacterial species, Escherichia coli and Haemophilus influenzae. Expression of each of these DNA fragments resu lted in the accumulation of the corresponding recombinant proteins in insoluble aggregates, Each recombinant protein was solubilised, refold ed and shown to be able to cleave synthetic peptides that have been ex tensively used previously as substrates for aspartic proteinases of ve rtebrate, fungal and retroviral origin, Each activity was completely b locked by the diagnostic aspartic proteinase inhibitor, acetyl-pepstat in, This is thus the first report demonstrating unequivocally that asp artic proteinases may be present in bacteria. (C) 1997 Federation of E uropean Biochemical Societies.