Open AccessExport without proteolytic processing of inner and outer membrane proteins encoded by F sex factor tra cistrons in Escherichia coli minicells.
Author(s) -
Mark Achtman,
Paul A. Manning,
Claus Edelbluth,
Peter Herrlich
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.10.4837
Subject(s) - inner membrane , bacterial outer membrane , escherichia coli , membrane protein , cytoplasm , biology , outer membrane efflux proteins , cleavage (geology) , membrane , microbiology and biotechnology , biochemistry , chemistry , gene , paleontology , fracture (geology)
Most tra proteins encoded by the Escherichia coli F sex factor are incorporated into the minicell envelope. We have now assigned the tra proteins to cytoplasm (TraIp and 2b), inner membrane (TraEp, TraMp, and TraSp), and outer membrane (6e, TraAp, TraBp, TraJp, TraKp, TraLp, and TraTp). two proteins, TraDp and 6d, were associated with both inner and outer membranes. The proteins exported to the inner or outer membranes did not undergo proteolytic cleavage (processing) whereas beta-lactamase was processed normally.