Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coli.
Open Access
- 1 February 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (3) , 1836-1841
- https://doi.org/10.1016/s0021-9258(18)89669-7
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteinsCell, 1984
- Signal sequence mutations disrupt feedback between secretion of an exported protein and its synthesis in E. coliNature, 1984
- M13 coat protein as a model of membrane assemblyTrends in Biochemical Sciences, 1983
- Mechanism of Incorporation of Cell Envelope Proteins in Escherichia ColiAnnual Review of Microbiology, 1982
- In vitro synthesis of the membrane-bound D-lactate dehydrogenase of Escherichia coliBiochemistry, 1982
- Membrane assembly from purified components. II. Assembly of M13 procoat into liposomes reconstituted with purified leader peptidaseCell, 1981
- Different exported proteins in E. coli show differences in the temporal mode of processing in vivoCell, 1981
- In vitro synthesis of the respiratory dehydrogenase of Escherichia coli. Role of UUG as initiation codonBiochemistry, 1981
- Sequence of the lactose permease geneNature, 1980
- The Major Proteins of the Escherichia coli Outer Cell Envelope Membrane. Preparative Isolation of All Major Membrane ProteinsEuropean Journal of Biochemistry, 1975