Open AccessCloning and characterization of an extracellular temperature‐labile serine protease gene from Aeromonas hydrophila
Author(s) -
Rivero Octavio,
Anguita Juan,
Mateos Diana,
Paniagua Carmen,
Naharro Germán
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04702.x
Subject(s) - aeromonas hydrophila , serine protease , proteases , biology , microbiology and biotechnology , molecular cloning , escherichia coli , aeromonas , protease , gene , pseudomonas putida , plasmid , biochemistry , bacteria , peptide sequence , genetics , enzyme
Aeromonas virulence is thought to depend on multigenic functions. The gene for an extracellular protease from Aeromonas hydrophila SO2/2 was cloned in Escherichia coli C600‐1 by using pIJ860, bifunctional plasmid, as a vector. The gene encodes for a temperature‐labile serine protease (P2) with a molecular mass of approx. 68 kDa which is highly inhibited by PMSF. The gene was expressed in Streptomyces lividans 1326 by transforming protoplasts with the original clone pPA2. We were also able to transfer and express the prt P2 gene in Pseudomonas putida by mating experiments. The protein P2 was secreted into the periplasms of both P. putida and E. coli C600‐1 being identical in properties to one of the proteases secreted into the culture supernatant by A. hydrophila SO2/2.