Distinct Membrane Binding Properties of N- and C-terminal Domains of Escherichia coli SecA ATPase

This publication has 68 references indexed in Scilit:

• TARGETING AND ASSEMBLY OF PERIPLASMIC AND OUTER-MEMBRANE PROTEINS IN ESCHERICHIA COLI
  Annual Review of Genetics, 1998
• The Sec system
  Current Opinion in Microbiology, 1998
• Protein Translocation in the Three Domains of Life: Variations on a Theme
  Cell, 1997
• Integration of SecA protein into the Escherichia coli inner membrane is regulated by its amino‐terminal ATP‐binding domain
  Molecular Microbiology, 1996
• SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF
  Cell, 1995
• Two distinct ATP‐binding domains are needed to promote protein export by Escherichia coli SecA ATPase
  Molecular Microbiology, 1993
• SecY and integral membrane components of the Escherichia coli protein translocation system
  Molecular Microbiology, 1992
• The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane
  Cell, 1990
• The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins
  Cell, 1990
• SecA protein is required for secretory protein translocation into E. coli membrane vesicles
  Cell, 1988