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• W285247018 endingPage "74" @default.
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• W285247018 abstract "Abstract Structural characteristics of the signal peptide domains and the mature domain of presecretory proteins are discussed in relation to the translocation competence of these proteins. The signal peptide domain is characterized by an amino terminal positive charge and a central hydrophobic stretch, both of which play important roles in protein translocation. Functions of the two parts are interrelated. Evidence suggesting that the two regions are recognized specifically by components of the secretory machinery is presented. The chemical structure of the signal peptide cleavage site and its possible implication in translocation competence are also discussed. Although translocation of the mature region is a rather passive process, the structure of this domain affects the translocation competence. A long hydrophobic stretch blocks ongoing translocation. The presence of positively charged residues near the amino terminus of the mature domain also inhibits translocation. Evidence has accumulated indicating that the mature region does not necessarily have to be an expanded linear polypeptide chain; polypeptide chains intramolecularly cross-linked to form a loop of a certain size or a mature domain composed of two polypeptide chains, which are cross-linked with relatively large cross-linkers, are also translocation competent. Based on these facts, the mechanism underlying the translocation of presecretory proteins is discussed." @default.
• W285247018 created "2016-06-24" @default.
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• W285247018 date "1992-01-01" @default.
• W285247018 modified "2023-10-01" @default.
• W285247018 title "Chapter 6 Structural characteristics of presecretory proteins: their implication as to translocation competency" @default.
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• W285247018 doi "https://doi.org/10.1016/s0167-7306(08)60083-6" @default.
• W285247018 hasPublicationYear "1992" @default.
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