Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12).

This publication has 27 references indexed in Scilit:

• Escherichia coliSecY and SecE proteins appear insufficient to constitute the SecA receptor
  FEBS Letters, 1994
• Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
  Cell, 1993
• Purified Escherichia coli preprotein translocase catalyzes multiple cycles of precursor protein translocation
  Biochemistry, 1993
• Overproduction, purification and characterization of SecD and SecF, integral membrane components of the protein translocation machinery of Escherichia coli
  Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1992
• SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study
  Biochemistry, 1992
• Purification of SecE and reconstitution of SecE‐dependent protein translocation activity
  FEBS Letters, 1991
• Reconstitution of translocation activity for secretory proteins from solubilized components of Escherichia coli
  European Journal of Biochemistry, 1990
• SecE‐dependent overproduction of SecY in Escherichia coli
  FEBS Letters, 1990
• The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins
  Cell, 1990
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970