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Translocation of colicin E1 through cytoplasmic membrane of Escherichia coli
Author(s) -
Yamada Mamoru,
Miki Toru,
Nakazawa Atsushi
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80790-4
Subject(s) - colicin , chromosomal translocation , bacterial outer membrane , escherichia coli , fusion protein , mutant , chemistry , inner membrane , lac operon , cytoplasm , maltose binding protein , gene product , biology , biochemistry , microbiology and biotechnology , gene , membrane , gene expression , recombinant dna
The product of the malE—lacZ gene fusion was reported to compete with some proteins including outer membrane lipoprotein in the protein translocation across the Echerichia coli membrane. The fusion product also inhibited colicin E1 export. Furthermore, globomycin, which accumulated prolipoprotein in the membrane, inhibited the translocation of colicin E1 in the wild‐type cells, but not in lipoprotein‐negative mutant cells. Since colicin E1 contains the internal signal‐like sequence [Proc. Natl. Acad. Sci. USA (1982) 79, 2827–2831], these results suggest that colicin E1 is exported by the aid of this sequence at a common site for maltose‐binding protein and lipoprotein translocation.