Secretion and processing of ribose-binding protein in Escherichia coli

Abstract

The periplasmic D-ribose-binding protein of E. 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 protein have many characteristics in common.