The Protein Translocation Apparatus Contributes to Determining the Topology of an Integral Membrane Protein in Escherichia coli
Open Access
- 1 April 1998
- journal article
- Published by Elsevier
- Vol. 273 (14) , 8419-8424
- https://doi.org/10.1074/jbc.273.14.8419
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Insertion of the Polytopic Membrane Protein MalF Is Dependent on the Bacterial Secretion MachineryJournal of Biological Chemistry, 1996
- Heads or tails — what determines the orientation of proteins in the membraneFEBS Letters, 1995
- Building bridges: disulphide bond formation in the cellMolecular Microbiology, 1994
- Requirements for translocation of periplasmic domains in polytopic membrane proteinsJournal of Bacteriology, 1994
- Membrane topology of the pBR322 tetracycline resistance protein. TetA-PhoA gene fusions and implications for the mechanism of TetA membrane insertion.Journal of Biological Chemistry, 1992
- Export of maltose-binding protein species with altered charge distribution surrounding the signal peptide hydrophobic core in Escherichia coli cells harboring prl suppressor mutationsJournal of Bacteriology, 1992
- The role of charged amino acids in the localization of secreted and membrane proteinsCell, 1990
- Control of topology and mode of assembly of a polytopic membrane protein by positively charged residuesNature, 1989
- The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topologyThe EMBO Journal, 1986
- Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteinsCell, 1984