The C Terminus of SecA Is Involved in Both Lipid Binding and SecB Binding
Open Access
- 1 April 1995
- journal article
- Published by Elsevier BV
- Vol. 270 (14), 7902-7907
- https://doi.org/10.1074/jbc.270.14.7902
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Carboxy-Terminal Region of Escherichia coli SecA ATPase Is Important to Promote Its Protein Translocation Activity in VivoBiochemical and Biophysical Research Communications, 1994
- Nucleotide and negatively charged lipid‐dependent vesicle aggregation caused by SecAFEBS Letters, 1993
- The components of the Escherichia coli protein-transport apparatus: Current Opinion in Structural Biology 1993, 3:541–546Current Opinion in Structural Biology, 1993
- Phosphatidylglycerol dependent protein translocation across the Escherichia coli inner membrane is inhibited by the anti‐cancer drug doxorubicinFEBS Letters, 1993
- Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative StructureScience, 1992
- SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer studyBiochemistry, 1992
- SecA, an essential component of the secretory machinery of Escherichiacoli, exists as homodimerBiochemical and Biophysical Research Communications, 1991
- Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranesNature, 1988
- Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genesJournal of Molecular Biology, 1986
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976