Non-specific hole formation in the Escherichia coli inner membrane by lambda S proteins in independent of cellular secY and secA functions and of the proportion of membrane acidic phospholipids.
Formation of the lesion in the Escherichia coli inner membrane caused by lambda lysis protein S was examined by electron microscopy. We also show that macromolecules exceeding the size of the lambda R transglycosylase can pass through the S-dependent hole and that assembly of the S-dependent hole is independent of the proportion of acidic phospholipids in the inner membrane and of components of the cellular transport machinery.
Rietsch
A
A
Institute of Microbiology and Genetics, University of Vienna, Austria.
Bläsi
U
U
D000251:Adenosine Triphosphatases / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D010582:Bacteriophage lambda / Q000235:genetics / Q000502:physiology*; D001692:Biological Transport; D002462:Cell Membrane; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics*; D029968:Escherichia coli Proteins; D016695:Glycosyltransferases; D008563:Membrane Lipids / Q000032:analysis*; D026901:Membrane Transport Proteins; D010743:Phospholipids / Q000032:analysis*; D000069816:SEC Translocation Channels; D000081416:SecA Proteins; D013104:Spheroplasts / Q000378:metabolism; D014166:Transferases / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008563:Membrane Lipids; D026901:Membrane Transport Proteins; D010743:Phospholipids; D000069816:SEC Translocation Channels; C057841:SecY protein, E coli; D014764:Viral Proteins; D014166:Transferases; D016695:Glycosyltransferases; C021815:murein transglycosylase; D000251:Adenosine Triphosphatases; D000081416:SecA Proteins