Pro-OmpA Derivatives with a His6 Tag in Their N-terminal “Translocation Initiation Domains” Are Arrested by Ni2+ at an Early Post-targeting Stage of Translocation

This publication has 32 references indexed in Scilit:

• A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
  Cell, 1995
• Biochemical characterization of the presecretory protein translocation machinery ofEscherichia coli
  FEBS Letters, 1994
• The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation
  Cell, 1993
• A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation
  Cell, 1992
• SecY variants that interfere with Escherichia coli protein export in the presence of normal secY
  Molecular Microbiology, 1992
• The signal sequence receptor has a second subunit and is part of a translocation complex in the endoplasmic reticulum as probed by bifunctional reagents.
  The Journal of cell biology, 1990
• The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane
  Cell, 1990
• The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocation
  Cell, 1990
• The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins
  Cell, 1990
• A C-terminal signal prevents secretion of luminal ER proteins
  Published by Elsevier ,1987