We have studied the export kinetics of the maltose-binding protein (MBP) of Escherichia coli, the malE gene product, when it is synthesized with either a wildtype signal sequence or with a mutationally altered signal sequence that affects the efficiency of secretion to the periplasm. Our results confirm a very rapid export process for the wild-type protein and, in contrast, reveal a relatively slow post-translational mode of export for the altered precursor species. For each different signal sequence mutant, a fraction of the precursor MBP pool that is proportional to the strength of the export defect appears to never exit the cytoplasm. We have also analyzed MBP export in strains harboring prl mutations that suppress malE signal sequence mutations and are thought to somehow alter the specificity of the cell's protein export machinery. The introduction of different prl alleles has no apparent effect on wild-type MBP export but increases both the amount of mutant MBP that is exported and the rate at which this is accomplished. In fact, the presence of two different prl alleles in the same strain can act synergistically in suppressing MBP export defects. The inhibition of total protein synthesis with chloramphenicol can also increase the proportion of pMBP that is post-translationally exported in these strains. A model that describes the initial steps in MBP export is presented.