Membrane trigger hypothesis

Structural organization of the plasma membrane Membrane assembly in vitro The membrane trigger hypothesis Transport of proteins into mitochondria... 

The role of catalysis in membrane assembly is emphasized again by the above model since the N-terminal sequence of the nascent polypeptide chain of a spanning protein is released by proteolysis as soon as it reaches the cytosol. The N-terminal polypeptide chain extension may help the chain penetrate the hydrophobic bilayer and solubilize the resulting hydrophobic N-terminal part of the chain in the aqueous medium of the cytoplasm. However, the role of the protease-catalyzed hydrolysis of the polypeptide chain in membrane assembly is minimized in the membrane trigger hypothesis (99). According to this model, the essential role of the leader sequence would be to modify, in association with the lipid bilayer, the folding pathway of the protein in such a way that the polypeptide chain could span the membrane. 

Wickner (1980) proposed an alternative mechanism of protein secretion, called the membrane trigger hypothesis. This model proposes that the signal sequence influences the precursor protein or a domain of the precursor to fold into a conformation that can spontaneously partition into the hydrophobic part of the bilayer. In prokaryotes, the membrane potential causes the protein to traverse the bilayer. The protein then regains a water-soluble conformation, and is expelled into the medium. Signal peptidase removes the signal sequence during or after this process. Thus, secretory proteins or domains are transported across the membrane posttranslationally without the aid of a proteinaceous secretory apparatus. An energy source, such as the membrane potential, is required for secretion. 

Exported proteins must cross a biological membrane, which is composed largely of lipids and proteins. Is the translocation site made of lipids or protein The membrane trigger hypothesis, the helical hairpin hypothesis, the domain model, and the model of Nesmayanova postulate that protein translocation occurs directly through the lipid bilayer and that no proteinaceous export site is necessary. Other proteins may be needed for recognition, and signal peptidase is required for removal of the signal sequence after export. Evidence for a lipid translocation site comes primarily from experiments in reconstituted export systems in Wickner s laboratory. It has been shown that the precursors of M13... 

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