TY - JOUR
T1 - Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysin HlyB and HlyD
AU - Suh, Y.
AU - Benedik, M. J.
PY - 1992
Y1 - 1992
N2 - Serratia marcescens produces an abundant extracellular metalloprotease. The gene for this protease had previously been cloned and expressed in Escherichia coli, in which no functional protease could be found. However, the protease gene carries the LXGGXGND repeat motif found in α-hemolysin and other proteins secreted by homologous systems. Using a dual-plasmid complementation system, we show that the α-hemolysin hlyB and hlyD transport determinants are sufficient to allow secretion and activation of a functional metalloprotease species from E. coli, as are the comparable protease secretion functions of Erwinia chrysanthemi. However, strains expressing protease with the hlyBD transport system are unstable and rapidly lose the ability to produce functional protease.
AB - Serratia marcescens produces an abundant extracellular metalloprotease. The gene for this protease had previously been cloned and expressed in Escherichia coli, in which no functional protease could be found. However, the protease gene carries the LXGGXGND repeat motif found in α-hemolysin and other proteins secreted by homologous systems. Using a dual-plasmid complementation system, we show that the α-hemolysin hlyB and hlyD transport determinants are sufficient to allow secretion and activation of a functional metalloprotease species from E. coli, as are the comparable protease secretion functions of Erwinia chrysanthemi. However, strains expressing protease with the hlyBD transport system are unstable and rapidly lose the ability to produce functional protease.
UR - http://www.scopus.com/inward/record.url?scp=0026560394&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026560394&partnerID=8YFLogxK
U2 - 10.1128/jb.174.7.2361-2366.1992
DO - 10.1128/jb.174.7.2361-2366.1992
M3 - Article
C2 - 1551853
AN - SCOPUS:0026560394
SN - 0021-9193
VL - 174
SP - 2361
EP - 2366
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 7
ER -