文摘
Understanding the transport of hydrophilic proteins across biological membranes continues tobe an important undertaking. The general secretory (Sec) pathway in Escherichia coli transports the majorityof E. coli proteins from their point of synthesis in the cytoplasm to their sites of final localization, associatingsequentially with a number of protein components of the transport machinery. The targeting signals forthese substrates must be discriminated from those of proteins transported via other pathways. While targetingsignals for each route have common overall characteristics, individual signal peptides vary greatly intheir amino acid sequences. How do these diverse signals interact specifically with the proteins that comprisethe appropriate transport machinery and, at the same time, avoid targeting to an alternate route? Therecent publication of the crystal structures of components of the Sec transport machinery now allows amore thorough consideration of the interactions of signal sequences with these components.