Abstract
In this study, using a derivative of proOmpA containing an artificial stop-transfer sequence (proOmpA2xH1), we analyzed the process of stop-transfer during translocation across the cytoplasmic membrane of Escherichia coli. ProOmpA2xH1 did not interfere with the transit of wild-type proOmpA. When proOmpA2xH1 was anchored in the membrane, membrane-inserted SecA was deinserted with the reversion of the inverted topology of SecG. Cross-linking experiments revealed that the anchored proOmpA2xH1 that does not interact with either SecY or SecA. These results, taken together, suggest that proOmpA2xH1 leaves the translocation pathway by means of a specific interaction between the stop-transfer sequence and the translocational channel.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenosine Triphosphate / metabolism
-
Bacterial Outer Membrane Proteins / chemistry
-
Bacterial Outer Membrane Proteins / metabolism*
-
Bacterial Proteins / metabolism
-
Binding Sites
-
Biological Transport
-
Cytoplasm / metabolism
-
Escherichia coli / metabolism*
-
Escherichia coli Proteins*
-
Hydrolysis
-
Intracellular Membranes / metabolism
-
Membrane Proteins / metabolism
-
Protein Conformation
-
Protein Precursors / chemistry
-
Protein Precursors / metabolism*
-
SEC Translocation Channels
Substances
-
Bacterial Outer Membrane Proteins
-
Bacterial Proteins
-
Escherichia coli Proteins
-
Membrane Proteins
-
Protein Precursors
-
SEC Translocation Channels
-
SecG protein, E coli
-
outer membrane protein A precursor (E coli)
-
Adenosine Triphosphate