Abstract:
:The chromosomal gef gene of Escherichia coli is a member of the gef gene family which encodes strongly toxic proteins of about 50 amino acids. We demonstrate here that the Gef protein is detectable by anti-peptide antibodies. Furthermore, we show that Gef is anchored in the cytoplasmic membrane by the N-terminal part of the protein, and that the C-terminal part is localized in the periplasm in a dimeric form with at least one disulphide bond. By mutagenesis of gef it is shown that the periplasmic portion of Gef encodes the toxic domain and that the dimerization of Gef is not essential for the toxic effect.
journal_name
Mol Microbioljournal_title
Molecular microbiologyauthors
Poulsen LK,Refn A,Molin S,Andersson Pdoi
10.1111/j.1365-2958.1991.tb01910.xsubject
Has Abstractpub_date
1991-07-01 00:00:00pages
1627-37issue
7eissn
0950-382Xissn
1365-2958journal_volume
5pub_type
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