Secretion and processing of ribose-binding protein in Escherichia coli.

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RESUMO

The periplasmic D-ribose-binding protein of Escherichia coli K-12 is made initially as a larger precursor form. This precursor was observed in wild-type cells and more stably in cells inhibited for protein secretion. The precursor could be processed to the mature D-ribose-binding protein either co-or posttranslationally. The secretion pathway of the D-ribose-binding protein and that of the maltose-binding secretion have many characteristics in common.

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