The penicillinase of Bacillus licheniformis is an outer membrane protein in Escherichia coli.

Abstract:

:The cloned gene coding for Bacillus licheniformis penicillinase (penP) was introduced into Escherichia coli in a heat-inducible lambda Qam vector. After induction, significant amounts of penicillinase were synthesized in the new host. The cellular location of the penicillinase was found to be almost exclusively the outer membrane fraction of E. coli, and virtually no soluble penicillinase was found. According to sodium dodecyl sulfate-gel electrophoresis, the size of the penicillinase from E. coli was identical to that of the membrane-bound form of the B. licheniformis penicillinase. Gel filtration in the presence of Triton X-100 suggested that the penicillinase from E. coli had amphiphilic properties, as does B. licheniformis membrane penicillinase. These results show that the export of the penicillinase to the outer membrane of E. coli involves the cleavage of the signal peptide from the prepenicillinase, giving an outer membrane component indistinguishable from the membrane penicillinase of B. licheniformis.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Sarvas MO,Palva IA

doi

10.1128/JB.155.2.657-663.1983

subject

Has Abstract

pub_date

1983-08-01 00:00:00

pages

657-63

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

155

pub_type

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