Abstract:
:Erwinia chrysanthemi, a phytopathogenic bacterium, produces a protease inhibitor which is a low-molecular-weight, heat-stable protein. In addition to its action on the three E. chrysanthemi extracellular proteases A, B and C, it also strongly inhibits the 50 kD extracellular protease of Serratia marcescens. Its structural gene (inh) was subcloned and expressed in Escherichia coli, in which it encodes an active inhibitor which was purified. The nucleotide sequence of the inh gene shows an open reading frame of 114 condons. The N-terminal amino acid sequence of the purified inhibitor was also determined. It indicated the existence of an amino-terminal signal peptide absent from the mature protein. The inhibitor is entirely periplasmic in E. chrysanthemi and partially periplasmic in E. coli.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Létoffé S,Delepelaire P,Wandersman Cdoi
10.1111/j.1365-2958.1989.tb00106.xsubject
Has Abstractpub_date
1989-01-01 00:00:00pages
79-86issue
1eissn
0950-382Xissn
1365-2958journal_volume
3pub_type
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