Modulation of folding pathways of exported proteins by the leader sequence

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Science  26 Feb 1988:
Vol. 239, Issue 4843, pp. 1033-1035
DOI: 10.1126/science.3278378


Leader peptides that function to direct export of proteins through membranes have some common features but exhibit a remarkable sequence diversity. Thus there is some question whether leader peptides exert their function through conventional stereospecific protein-protein interaction. Here it is shown that the leader peptides retarded the folding of precursor maltose-binding protein and ribose-binding protein from Escherichia coli. This kinetic effect may be crucial in allowing precursors to enter the export pathway.