Dependence of secretion and assembly of type 1 fimbrial subunits of Escherichia coli on normal protein export.
The export of fimbrial subunits was found to be diminished at the restrictive temperature in a strain bearing a secA(Ts) mutation. Likewise, export was inhibited in a strain harboring a malE-lacZ protein fusion upon induction of hybrid protein synthesis. Both conditions resulted in the accumulation of a precursor protein ca. 2,000 daltons larger than the mature fimbrial subunit.
D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics* / Q000648:ultrastructure; D029968:Escherichia coli Proteins; D010861:Fimbriae, Bacterial / Q000648:ultrastructure*; D005838:Genotype; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D009004:Monosaccharide Transport Proteins; D009154:Mutation; D033902:Periplasmic Binding Proteins; D013696:Temperature
D018528:ATP-Binding Cassette Transporters; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C461619:MalE protein, E coli; D058619:Maltose-Binding Proteins; D008565:Membrane Proteins; D009004:Monosaccharide Transport Proteins; D033902:Periplasmic Binding Proteins; C461599:maltose transport system, E coli