Abstract:
:Subtilin is an antimicrobial peptide of the lantibiotic family that is produced by Gram-positive Bacillus subtilis, and its biosynthesis involves expression of presubtilin which consists of a leader segment and a mature segment. The leader segment is unlike a typical sec-type general secretion signal, and its ability to mediate translocation through a non-sec pathway has been previously studied by fusing the subtilin leader to an alkaline phosphatase reporter and expressing it in B. subtilis 168 [Izaguirre, G. and Hansen, J. N. (1997) Appl. Environ. Microbiol. 63, 3965-3971]. In this work, we have expressed the same subtilin leader-AP fusion in Gram-negative Escherichia coli, and found that the AP polypeptide is translocated into the periplasmic compartment and assembles into an enzymatically active form. The subtilin leader segment was not cleaved from this enzymatically active AP, which remained associated with the membrane. Conversion of the cells to spheroplasts followed by treatment with proteinase K showed that about 50% of the bound AP was sufficiently exposed on the surface of the spheroplasts to be inactivated by proteolytic cleavage.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Paul LK,Izaguirre G,Hansen JNdoi
10.1111/j.1574-6968.1999.tb13640.xkeywords:
subject
Has Abstractpub_date
1999-07-01 00:00:00pages
45-50issue
1eissn
0378-1097issn
1574-6968pii
S0378-1097(99)00217-7journal_volume
176pub_type
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