Open AccessSynthesis of phage M13 coat protein and its assembly into membranes in vitro.
Author(s) -
William Wickner,
Gail Mandel,
Craig Zwizinski,
Marjorie Bates,
Teresa Killick
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.4.1754
Subject(s) - liposome , escherichia coli , peptide , vesicle , bilayer , integral membrane protein , membrane , vesicle associated membrane protein 8 , lipid bilayer , bacteriophage , membrane protein , biophysics , chemistry , biochemistry , in vitro , biology , gene
The coat protein (gene 8 product) of coliphage M1O is an integral protein of the host cell membrane at all stages of virus infection. This protein, when made in a cell-free reaction, has been shown by others to have an additional NH2-terminal peptide region and is referred to as "procoat." It is initially not membrane-bound but, upon exposure to Escherichia coli membrane vesicles or to liposomes prepared from E. coli lipids, it assembles into the bilayer in an integral fashion. Much of this protein is shown to be exposed on the inner surface of the liposome. We suggest that refolding of procoat as it encounters the bilayer is sufficient to transport large segments of the peptide chain through the apolar hydrocarbon core.