Abstract
New insights into how proteins cross membranes are beginning to emerge. Although there is no universal mechanism, recent results suggest that there are common features of protein translocation. Three steps usually are involved : i) the association of the protein with receptors on the correct membrane, ii) the translocation through the membrane and iii) covalent modification and folding on the opposite membrane surface. A requirement which has now been well established is that the unfolded state of the polypeptide chain to be transferred has to be maintained. By unfolded we mean that this polypeptide has not attained its final most stable conformation although it has obviously acquired some secondary structure. Therefore, an essential feature of translocation may have to do with preventing the folding of the protein into a tertiary structure approximating that of the mature protein. This feature has been demonstrated in mitochondria with dihydrofolate reductase fused with the cytochrome oxydase subunit IV (Eilers and Schatz, 1986), in E. coli with the phosphate binding protein (Pagès et al., 1984) and the maltose binding protein (Randall and Hardy, 1986) and in the rough endoplasmic reticulum with preprolactin by Maher and Singer (1986).
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Lazdunski, C.J. (1988). What Can We Learn from Colicins about the Dynamics of Insertion and Transfer of Proteins into and Across Membranes. In: Op den Kamp, J.A.F. (eds) Membrane Biogenesis. NATO ASI Series, vol 16. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73184-6_24
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DOI: https://doi.org/10.1007/978-3-642-73184-6_24
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