SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.

This publication has 33 references indexed in Scilit:

• The role of the positively charged N-terminus of the signal sequence of E. coli outer membrane protein PhoE in export
  Biochimica et Biophysica Acta (BBA) - Biomembranes, 1989
• SecA protein is directly involved in protein secretion in Escherichia coli
  FEBS Letters, 1989
• SecA suppresses the temperature-sensitive SecY24 defect in protein translocation in Escherichia coli membrane vesicles.
  Proceedings of the National Academy of Sciences, 1988
• SecA protein is required for secretory protein translocation into E. coli membrane vesicles
  Cell, 1988
• Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
  Nature, 1988
• Export of Protein: A Biochemical View
  Annual Review of Microbiology, 1987
• A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins
  Cell, 1983
• The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
  Gene, 1982
• Regulation of a membrane component required for protein secretion in escherichia coli
  Cell, 1982
• E. coli mutant pleiotropically defective in the export of secreted proteins
  Cell, 1981